data_9JI7
# 
_entry.id   9JI7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JI7         pdb_00009ji7 10.2210/pdb9ji7/pdb 
WWPDB D_1300051304 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JI7 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 liyaoyao@sdu.edu.cn Yaoyao Li  ? 'principal investigator/group leader' 0000-0002-8762-9615 
5 zhudeyu@sdu.edu.cn  Deyu   Zhu ? 'principal investigator/group leader' 0000-0002-2949-9410 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, Y.'  1 0000-0002-8762-9615 
'Zhu, D.' 2 0000-0002-2949-9410 
'Xie, X.' 3 0000-0002-5118-6111 
'Li, F.'  4 0009-0009-0724-7915 
'Lu, M.'  5 0009-0000-1359-6323 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                19253 
_citation.page_last                 19261 
_citation.title                     
;Structural Basis for Medium-Chain Dehydrogenase/Reductase-Catalyzed Reductive Cyclization in Polycyclic Tetramate Macrolactam Biosynthesis.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.5c04971 
_citation.pdbx_database_id_PubMed   40406958 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xie, X.'  1  0000-0002-5118-6111 
primary 'Li, F.'   2  ?                   
primary 'Mu, Y.'   3  ?                   
primary 'Lu, M.'   4  ?                   
primary 'Luo, J.'  5  ?                   
primary 'Wang, H.' 6  0000-0002-1779-0286 
primary 'Shen, Y.' 7  0000-0002-3881-0135 
primary 'Du, L.'   8  0000-0003-4048-1008 
primary 'Zhu, D.'  9  0000-0002-2949-9410 
primary 'Li, Y.'   10 0000-0002-8762-9615 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'NADP-dependent oxidoreductase' 38943.332 2   ? ? ? ? 
2 non-polymer syn 
;(1Z,3E,5E,7S,8R,9S,10S,11R,13R,15S,16Z,18E,24S)-11-ethyl-2,7-dihydroxy-10-methyl-21,25-diazatetracyclo[22.2.1.08,15.09,13]heptacosa-1,3,5,16,18-pentaene-20,26,27-trione
;
494.622   2   ? ? ? ? 
3 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   2   ? ? ? ? 
4 water       nat water 18.015    148 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Oxidoreductase,zinc-binding dehydrogenase family protein' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;LGSMKTERWVVREHVEGVPDAARIYEKVETELNTRLGEEQMLLKTLYVSVDPYLQGICLDTPIGDHMGADSIMQVLDAGP
NAPFRPGDLVQGFGGWRTHLVSDGKPKLWQTGTFPMVFPAYRKLDLRHYDDALPLSTALGVMGGPGMTAWGTMTKFMQVR
PGDTVVVSGASGMIGTLVGQMAKRAGARVVGTAGSAGKARYLSQLGFDAVIDYKLADDADKMREALREAAPDGVDKYFDS
IGGSVTDAVFSMLNVGSQVAVCWQWATQVQRDYHGPRLLPYIMFPRATIRGIFSLEWFTEQNWSALHEELGGLVRRQELV
AHETVQDGFEHIPAAYQTLFSASESNRGKVLVRV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LGSMKTERWVVREHVEGVPDAARIYEKVETELNTRLGEEQMLLKTLYVSVDPYLQGICLDTPIGDHMGADSIMQVLDAGP
NAPFRPGDLVQGFGGWRTHLVSDGKPKLWQTGTFPMVFPAYRKLDLRHYDDALPLSTALGVMGGPGMTAWGTMTKFMQVR
PGDTVVVSGASGMIGTLVGQMAKRAGARVVGTAGSAGKARYLSQLGFDAVIDYKLADDADKMREALREAAPDGVDKYFDS
IGGSVTDAVFSMLNVGSQVAVCWQWATQVQRDYHGPRLLPYIMFPRATIRGIFSLEWFTEQNWSALHEELGGLVRRQELV
AHETVQDGFEHIPAAYQTLFSASESNRGKVLVRV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(1Z,3E,5E,7S,8R,9S,10S,11R,13R,15S,16Z,18E,24S)-11-ethyl-2,7-dihydroxy-10-methyl-21,25-diazatetracyclo[22.2.1.08,15.09,13]heptacosa-1,3,5,16,18-pentaene-20,26,27-trione
;
A1EBZ 
3 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP   
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LEU n 
1 2   GLY n 
1 3   SER n 
1 4   MET n 
1 5   LYS n 
1 6   THR n 
1 7   GLU n 
1 8   ARG n 
1 9   TRP n 
1 10  VAL n 
1 11  VAL n 
1 12  ARG n 
1 13  GLU n 
1 14  HIS n 
1 15  VAL n 
1 16  GLU n 
1 17  GLY n 
1 18  VAL n 
1 19  PRO n 
1 20  ASP n 
1 21  ALA n 
1 22  ALA n 
1 23  ARG n 
1 24  ILE n 
1 25  TYR n 
1 26  GLU n 
1 27  LYS n 
1 28  VAL n 
1 29  GLU n 
1 30  THR n 
1 31  GLU n 
1 32  LEU n 
1 33  ASN n 
1 34  THR n 
1 35  ARG n 
1 36  LEU n 
1 37  GLY n 
1 38  GLU n 
1 39  GLU n 
1 40  GLN n 
1 41  MET n 
1 42  LEU n 
1 43  LEU n 
1 44  LYS n 
1 45  THR n 
1 46  LEU n 
1 47  TYR n 
1 48  VAL n 
1 49  SER n 
1 50  VAL n 
1 51  ASP n 
1 52  PRO n 
1 53  TYR n 
1 54  LEU n 
1 55  GLN n 
1 56  GLY n 
1 57  ILE n 
1 58  CYS n 
1 59  LEU n 
1 60  ASP n 
1 61  THR n 
1 62  PRO n 
1 63  ILE n 
1 64  GLY n 
1 65  ASP n 
1 66  HIS n 
1 67  MET n 
1 68  GLY n 
1 69  ALA n 
1 70  ASP n 
1 71  SER n 
1 72  ILE n 
1 73  MET n 
1 74  GLN n 
1 75  VAL n 
1 76  LEU n 
1 77  ASP n 
1 78  ALA n 
1 79  GLY n 
1 80  PRO n 
1 81  ASN n 
1 82  ALA n 
1 83  PRO n 
1 84  PHE n 
1 85  ARG n 
1 86  PRO n 
1 87  GLY n 
1 88  ASP n 
1 89  LEU n 
1 90  VAL n 
1 91  GLN n 
1 92  GLY n 
1 93  PHE n 
1 94  GLY n 
1 95  GLY n 
1 96  TRP n 
1 97  ARG n 
1 98  THR n 
1 99  HIS n 
1 100 LEU n 
1 101 VAL n 
1 102 SER n 
1 103 ASP n 
1 104 GLY n 
1 105 LYS n 
1 106 PRO n 
1 107 LYS n 
1 108 LEU n 
1 109 TRP n 
1 110 GLN n 
1 111 THR n 
1 112 GLY n 
1 113 THR n 
1 114 PHE n 
1 115 PRO n 
1 116 MET n 
1 117 VAL n 
1 118 PHE n 
1 119 PRO n 
1 120 ALA n 
1 121 TYR n 
1 122 ARG n 
1 123 LYS n 
1 124 LEU n 
1 125 ASP n 
1 126 LEU n 
1 127 ARG n 
1 128 HIS n 
1 129 TYR n 
1 130 ASP n 
1 131 ASP n 
1 132 ALA n 
1 133 LEU n 
1 134 PRO n 
1 135 LEU n 
1 136 SER n 
1 137 THR n 
1 138 ALA n 
1 139 LEU n 
1 140 GLY n 
1 141 VAL n 
1 142 MET n 
1 143 GLY n 
1 144 GLY n 
1 145 PRO n 
1 146 GLY n 
1 147 MET n 
1 148 THR n 
1 149 ALA n 
1 150 TRP n 
1 151 GLY n 
1 152 THR n 
1 153 MET n 
1 154 THR n 
1 155 LYS n 
1 156 PHE n 
1 157 MET n 
1 158 GLN n 
1 159 VAL n 
1 160 ARG n 
1 161 PRO n 
1 162 GLY n 
1 163 ASP n 
1 164 THR n 
1 165 VAL n 
1 166 VAL n 
1 167 VAL n 
1 168 SER n 
1 169 GLY n 
1 170 ALA n 
1 171 SER n 
1 172 GLY n 
1 173 MET n 
1 174 ILE n 
1 175 GLY n 
1 176 THR n 
1 177 LEU n 
1 178 VAL n 
1 179 GLY n 
1 180 GLN n 
1 181 MET n 
1 182 ALA n 
1 183 LYS n 
1 184 ARG n 
1 185 ALA n 
1 186 GLY n 
1 187 ALA n 
1 188 ARG n 
1 189 VAL n 
1 190 VAL n 
1 191 GLY n 
1 192 THR n 
1 193 ALA n 
1 194 GLY n 
1 195 SER n 
1 196 ALA n 
1 197 GLY n 
1 198 LYS n 
1 199 ALA n 
1 200 ARG n 
1 201 TYR n 
1 202 LEU n 
1 203 SER n 
1 204 GLN n 
1 205 LEU n 
1 206 GLY n 
1 207 PHE n 
1 208 ASP n 
1 209 ALA n 
1 210 VAL n 
1 211 ILE n 
1 212 ASP n 
1 213 TYR n 
1 214 LYS n 
1 215 LEU n 
1 216 ALA n 
1 217 ASP n 
1 218 ASP n 
1 219 ALA n 
1 220 ASP n 
1 221 LYS n 
1 222 MET n 
1 223 ARG n 
1 224 GLU n 
1 225 ALA n 
1 226 LEU n 
1 227 ARG n 
1 228 GLU n 
1 229 ALA n 
1 230 ALA n 
1 231 PRO n 
1 232 ASP n 
1 233 GLY n 
1 234 VAL n 
1 235 ASP n 
1 236 LYS n 
1 237 TYR n 
1 238 PHE n 
1 239 ASP n 
1 240 SER n 
1 241 ILE n 
1 242 GLY n 
1 243 GLY n 
1 244 SER n 
1 245 VAL n 
1 246 THR n 
1 247 ASP n 
1 248 ALA n 
1 249 VAL n 
1 250 PHE n 
1 251 SER n 
1 252 MET n 
1 253 LEU n 
1 254 ASN n 
1 255 VAL n 
1 256 GLY n 
1 257 SER n 
1 258 GLN n 
1 259 VAL n 
1 260 ALA n 
1 261 VAL n 
1 262 CYS n 
1 263 TRP n 
1 264 GLN n 
1 265 TRP n 
1 266 ALA n 
1 267 THR n 
1 268 GLN n 
1 269 VAL n 
1 270 GLN n 
1 271 ARG n 
1 272 ASP n 
1 273 TYR n 
1 274 HIS n 
1 275 GLY n 
1 276 PRO n 
1 277 ARG n 
1 278 LEU n 
1 279 LEU n 
1 280 PRO n 
1 281 TYR n 
1 282 ILE n 
1 283 MET n 
1 284 PHE n 
1 285 PRO n 
1 286 ARG n 
1 287 ALA n 
1 288 THR n 
1 289 ILE n 
1 290 ARG n 
1 291 GLY n 
1 292 ILE n 
1 293 PHE n 
1 294 SER n 
1 295 LEU n 
1 296 GLU n 
1 297 TRP n 
1 298 PHE n 
1 299 THR n 
1 300 GLU n 
1 301 GLN n 
1 302 ASN n 
1 303 TRP n 
1 304 SER n 
1 305 ALA n 
1 306 LEU n 
1 307 HIS n 
1 308 GLU n 
1 309 GLU n 
1 310 LEU n 
1 311 GLY n 
1 312 GLY n 
1 313 LEU n 
1 314 VAL n 
1 315 ARG n 
1 316 ARG n 
1 317 GLN n 
1 318 GLU n 
1 319 LEU n 
1 320 VAL n 
1 321 ALA n 
1 322 HIS n 
1 323 GLU n 
1 324 THR n 
1 325 VAL n 
1 326 GLN n 
1 327 ASP n 
1 328 GLY n 
1 329 PHE n 
1 330 GLU n 
1 331 HIS n 
1 332 ILE n 
1 333 PRO n 
1 334 ALA n 
1 335 ALA n 
1 336 TYR n 
1 337 GLN n 
1 338 THR n 
1 339 LEU n 
1 340 PHE n 
1 341 SER n 
1 342 ALA n 
1 343 SER n 
1 344 GLU n 
1 345 SER n 
1 346 ASN n 
1 347 ARG n 
1 348 GLY n 
1 349 LYS n 
1 350 VAL n 
1 351 LEU n 
1 352 VAL n 
1 353 ARG n 
1 354 VAL n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   354 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GLE_3219 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Lysobacter enzymogenes' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     69 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1EBZ non-polymer         . 
;(1Z,3E,5E,7S,8R,9S,10S,11R,13R,15S,16Z,18E,24S)-11-ethyl-2,7-dihydroxy-10-methyl-21,25-diazatetracyclo[22.2.1.08,15.09,13]heptacosa-1,3,5,16,18-pentaene-20,26,27-trione
;
?                                            'C29 H38 N2 O5'     494.622 
ALA   'L-peptide linking' y ALANINE ?                                            'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ?                                            'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                                            'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                                            'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ?                                            'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE ?                                            'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                                            'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ?                                            'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE ?                                            'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ?                                            'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                                            'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ?                                            'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ?                                            'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ?                                            'C5 H11 N O2 S'     149.211 
NAP   non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
PHE   'L-peptide linking' y PHENYLALANINE ?                                            'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ?                                            'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ?                                            'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ?                                            'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                                            'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ?                                            'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ?                                            'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   LEU 1   -2  -2  LEU LEU A . n 
A 1 2   GLY 2   -1  -1  GLY GLY A . n 
A 1 3   SER 3   0   0   SER SER A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   LYS 5   2   2   LYS LYS A . n 
A 1 6   THR 6   3   3   THR THR A . n 
A 1 7   GLU 7   4   4   GLU GLU A . n 
A 1 8   ARG 8   5   5   ARG ARG A . n 
A 1 9   TRP 9   6   6   TRP TRP A . n 
A 1 10  VAL 10  7   7   VAL VAL A . n 
A 1 11  VAL 11  8   8   VAL VAL A . n 
A 1 12  ARG 12  9   9   ARG ARG A . n 
A 1 13  GLU 13  10  10  GLU GLU A . n 
A 1 14  HIS 14  11  11  HIS HIS A . n 
A 1 15  VAL 15  12  12  VAL VAL A . n 
A 1 16  GLU 16  13  13  GLU GLU A . n 
A 1 17  GLY 17  14  14  GLY GLY A . n 
A 1 18  VAL 18  15  15  VAL VAL A . n 
A 1 19  PRO 19  16  16  PRO PRO A . n 
A 1 20  ASP 20  17  17  ASP ASP A . n 
A 1 21  ALA 21  18  18  ALA ALA A . n 
A 1 22  ALA 22  19  19  ALA ALA A . n 
A 1 23  ARG 23  20  20  ARG ARG A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  TYR 25  22  22  TYR TYR A . n 
A 1 26  GLU 26  23  23  GLU GLU A . n 
A 1 27  LYS 27  24  24  LYS LYS A . n 
A 1 28  VAL 28  25  25  VAL VAL A . n 
A 1 29  GLU 29  26  26  GLU GLU A . n 
A 1 30  THR 30  27  27  THR THR A . n 
A 1 31  GLU 31  28  28  GLU GLU A . n 
A 1 32  LEU 32  29  29  LEU LEU A . n 
A 1 33  ASN 33  30  30  ASN ASN A . n 
A 1 34  THR 34  31  31  THR THR A . n 
A 1 35  ARG 35  32  32  ARG ARG A . n 
A 1 36  LEU 36  33  33  LEU LEU A . n 
A 1 37  GLY 37  34  34  GLY GLY A . n 
A 1 38  GLU 38  35  35  GLU GLU A . n 
A 1 39  GLU 39  36  36  GLU GLU A . n 
A 1 40  GLN 40  37  37  GLN GLN A . n 
A 1 41  MET 41  38  38  MET MET A . n 
A 1 42  LEU 42  39  39  LEU LEU A . n 
A 1 43  LEU 43  40  40  LEU LEU A . n 
A 1 44  LYS 44  41  41  LYS LYS A . n 
A 1 45  THR 45  42  42  THR THR A . n 
A 1 46  LEU 46  43  43  LEU LEU A . n 
A 1 47  TYR 47  44  44  TYR TYR A . n 
A 1 48  VAL 48  45  45  VAL VAL A . n 
A 1 49  SER 49  46  46  SER SER A . n 
A 1 50  VAL 50  47  47  VAL VAL A . n 
A 1 51  ASP 51  48  48  ASP ASP A . n 
A 1 52  PRO 52  49  49  PRO PRO A . n 
A 1 53  TYR 53  50  50  TYR TYR A . n 
A 1 54  LEU 54  51  51  LEU LEU A . n 
A 1 55  GLN 55  52  52  GLN GLN A . n 
A 1 56  GLY 56  53  53  GLY GLY A . n 
A 1 57  ILE 57  54  54  ILE ILE A . n 
A 1 58  CYS 58  55  55  CYS CYS A . n 
A 1 59  LEU 59  56  56  LEU LEU A . n 
A 1 60  ASP 60  57  57  ASP ASP A . n 
A 1 61  THR 61  58  58  THR THR A . n 
A 1 62  PRO 62  59  59  PRO PRO A . n 
A 1 63  ILE 63  60  60  ILE ILE A . n 
A 1 64  GLY 64  61  61  GLY GLY A . n 
A 1 65  ASP 65  62  62  ASP ASP A . n 
A 1 66  HIS 66  63  63  HIS HIS A . n 
A 1 67  MET 67  64  64  MET MET A . n 
A 1 68  GLY 68  65  65  GLY GLY A . n 
A 1 69  ALA 69  66  66  ALA ALA A . n 
A 1 70  ASP 70  67  67  ASP ASP A . n 
A 1 71  SER 71  68  68  SER SER A . n 
A 1 72  ILE 72  69  69  ILE ILE A . n 
A 1 73  MET 73  70  70  MET MET A . n 
A 1 74  GLN 74  71  71  GLN GLN A . n 
A 1 75  VAL 75  72  72  VAL VAL A . n 
A 1 76  LEU 76  73  73  LEU LEU A . n 
A 1 77  ASP 77  74  74  ASP ASP A . n 
A 1 78  ALA 78  75  75  ALA ALA A . n 
A 1 79  GLY 79  76  76  GLY GLY A . n 
A 1 80  PRO 80  77  77  PRO PRO A . n 
A 1 81  ASN 81  78  78  ASN ASN A . n 
A 1 82  ALA 82  79  79  ALA ALA A . n 
A 1 83  PRO 83  80  80  PRO PRO A . n 
A 1 84  PHE 84  81  81  PHE PHE A . n 
A 1 85  ARG 85  82  82  ARG ARG A . n 
A 1 86  PRO 86  83  83  PRO PRO A . n 
A 1 87  GLY 87  84  84  GLY GLY A . n 
A 1 88  ASP 88  85  85  ASP ASP A . n 
A 1 89  LEU 89  86  86  LEU LEU A . n 
A 1 90  VAL 90  87  87  VAL VAL A . n 
A 1 91  GLN 91  88  88  GLN GLN A . n 
A 1 92  GLY 92  89  89  GLY GLY A . n 
A 1 93  PHE 93  90  90  PHE PHE A . n 
A 1 94  GLY 94  91  91  GLY GLY A . n 
A 1 95  GLY 95  92  92  GLY GLY A . n 
A 1 96  TRP 96  93  93  TRP TRP A . n 
A 1 97  ARG 97  94  94  ARG ARG A . n 
A 1 98  THR 98  95  95  THR THR A . n 
A 1 99  HIS 99  96  96  HIS HIS A . n 
A 1 100 LEU 100 97  97  LEU LEU A . n 
A 1 101 VAL 101 98  98  VAL VAL A . n 
A 1 102 SER 102 99  99  SER SER A . n 
A 1 103 ASP 103 100 100 ASP ASP A . n 
A 1 104 GLY 104 101 101 GLY GLY A . n 
A 1 105 LYS 105 102 102 LYS LYS A . n 
A 1 106 PRO 106 103 103 PRO PRO A . n 
A 1 107 LYS 107 104 104 LYS LYS A . n 
A 1 108 LEU 108 105 105 LEU LEU A . n 
A 1 109 TRP 109 106 106 TRP TRP A . n 
A 1 110 GLN 110 107 107 GLN GLN A . n 
A 1 111 THR 111 108 108 THR THR A . n 
A 1 112 GLY 112 109 109 GLY GLY A . n 
A 1 113 THR 113 110 110 THR THR A . n 
A 1 114 PHE 114 111 111 PHE PHE A . n 
A 1 115 PRO 115 112 112 PRO PRO A . n 
A 1 116 MET 116 113 113 MET MET A . n 
A 1 117 VAL 117 114 114 VAL VAL A . n 
A 1 118 PHE 118 115 115 PHE PHE A . n 
A 1 119 PRO 119 116 116 PRO PRO A . n 
A 1 120 ALA 120 117 117 ALA ALA A . n 
A 1 121 TYR 121 118 118 TYR TYR A . n 
A 1 122 ARG 122 119 119 ARG ARG A . n 
A 1 123 LYS 123 120 120 LYS LYS A . n 
A 1 124 LEU 124 121 121 LEU LEU A . n 
A 1 125 ASP 125 122 122 ASP ASP A . n 
A 1 126 LEU 126 123 123 LEU LEU A . n 
A 1 127 ARG 127 124 124 ARG ARG A . n 
A 1 128 HIS 128 125 125 HIS HIS A . n 
A 1 129 TYR 129 126 126 TYR TYR A . n 
A 1 130 ASP 130 127 127 ASP ASP A . n 
A 1 131 ASP 131 128 128 ASP ASP A . n 
A 1 132 ALA 132 129 129 ALA ALA A . n 
A 1 133 LEU 133 130 130 LEU LEU A . n 
A 1 134 PRO 134 131 131 PRO PRO A . n 
A 1 135 LEU 135 132 132 LEU LEU A . n 
A 1 136 SER 136 133 133 SER SER A . n 
A 1 137 THR 137 134 134 THR THR A . n 
A 1 138 ALA 138 135 135 ALA ALA A . n 
A 1 139 LEU 139 136 136 LEU LEU A . n 
A 1 140 GLY 140 137 137 GLY GLY A . n 
A 1 141 VAL 141 138 138 VAL VAL A . n 
A 1 142 MET 142 139 139 MET MET A . n 
A 1 143 GLY 143 140 140 GLY GLY A . n 
A 1 144 GLY 144 141 141 GLY GLY A . n 
A 1 145 PRO 145 142 142 PRO PRO A . n 
A 1 146 GLY 146 143 143 GLY GLY A . n 
A 1 147 MET 147 144 144 MET MET A . n 
A 1 148 THR 148 145 145 THR THR A . n 
A 1 149 ALA 149 146 146 ALA ALA A . n 
A 1 150 TRP 150 147 147 TRP TRP A . n 
A 1 151 GLY 151 148 148 GLY GLY A . n 
A 1 152 THR 152 149 149 THR THR A . n 
A 1 153 MET 153 150 150 MET MET A . n 
A 1 154 THR 154 151 151 THR THR A . n 
A 1 155 LYS 155 152 152 LYS LYS A . n 
A 1 156 PHE 156 153 153 PHE PHE A . n 
A 1 157 MET 157 154 154 MET MET A . n 
A 1 158 GLN 158 155 155 GLN GLN A . n 
A 1 159 VAL 159 156 156 VAL VAL A . n 
A 1 160 ARG 160 157 157 ARG ARG A . n 
A 1 161 PRO 161 158 158 PRO PRO A . n 
A 1 162 GLY 162 159 159 GLY GLY A . n 
A 1 163 ASP 163 160 160 ASP ASP A . n 
A 1 164 THR 164 161 161 THR THR A . n 
A 1 165 VAL 165 162 162 VAL VAL A . n 
A 1 166 VAL 166 163 163 VAL VAL A . n 
A 1 167 VAL 167 164 164 VAL VAL A . n 
A 1 168 SER 168 165 165 SER SER A . n 
A 1 169 GLY 169 166 166 GLY GLY A . n 
A 1 170 ALA 170 167 167 ALA ALA A . n 
A 1 171 SER 171 168 168 SER SER A . n 
A 1 172 GLY 172 169 169 GLY GLY A . n 
A 1 173 MET 173 170 170 MET MET A . n 
A 1 174 ILE 174 171 171 ILE ILE A . n 
A 1 175 GLY 175 172 172 GLY GLY A . n 
A 1 176 THR 176 173 173 THR THR A . n 
A 1 177 LEU 177 174 174 LEU LEU A . n 
A 1 178 VAL 178 175 175 VAL VAL A . n 
A 1 179 GLY 179 176 176 GLY GLY A . n 
A 1 180 GLN 180 177 177 GLN GLN A . n 
A 1 181 MET 181 178 178 MET MET A . n 
A 1 182 ALA 182 179 179 ALA ALA A . n 
A 1 183 LYS 183 180 180 LYS LYS A . n 
A 1 184 ARG 184 181 181 ARG ARG A . n 
A 1 185 ALA 185 182 182 ALA ALA A . n 
A 1 186 GLY 186 183 183 GLY GLY A . n 
A 1 187 ALA 187 184 184 ALA ALA A . n 
A 1 188 ARG 188 185 185 ARG ARG A . n 
A 1 189 VAL 189 186 186 VAL VAL A . n 
A 1 190 VAL 190 187 187 VAL VAL A . n 
A 1 191 GLY 191 188 188 GLY GLY A . n 
A 1 192 THR 192 189 189 THR THR A . n 
A 1 193 ALA 193 190 190 ALA ALA A . n 
A 1 194 GLY 194 191 191 GLY GLY A . n 
A 1 195 SER 195 192 192 SER SER A . n 
A 1 196 ALA 196 193 193 ALA ALA A . n 
A 1 197 GLY 197 194 194 GLY GLY A . n 
A 1 198 LYS 198 195 195 LYS LYS A . n 
A 1 199 ALA 199 196 196 ALA ALA A . n 
A 1 200 ARG 200 197 197 ARG ARG A . n 
A 1 201 TYR 201 198 198 TYR TYR A . n 
A 1 202 LEU 202 199 199 LEU LEU A . n 
A 1 203 SER 203 200 200 SER SER A . n 
A 1 204 GLN 204 201 201 GLN GLN A . n 
A 1 205 LEU 205 202 202 LEU LEU A . n 
A 1 206 GLY 206 203 203 GLY GLY A . n 
A 1 207 PHE 207 204 204 PHE PHE A . n 
A 1 208 ASP 208 205 205 ASP ASP A . n 
A 1 209 ALA 209 206 206 ALA ALA A . n 
A 1 210 VAL 210 207 207 VAL VAL A . n 
A 1 211 ILE 211 208 208 ILE ILE A . n 
A 1 212 ASP 212 209 209 ASP ASP A . n 
A 1 213 TYR 213 210 210 TYR TYR A . n 
A 1 214 LYS 214 211 211 LYS LYS A . n 
A 1 215 LEU 215 212 212 LEU LEU A . n 
A 1 216 ALA 216 213 213 ALA ALA A . n 
A 1 217 ASP 217 214 214 ASP ASP A . n 
A 1 218 ASP 218 215 215 ASP ASP A . n 
A 1 219 ALA 219 216 216 ALA ALA A . n 
A 1 220 ASP 220 217 217 ASP ASP A . n 
A 1 221 LYS 221 218 218 LYS LYS A . n 
A 1 222 MET 222 219 219 MET MET A . n 
A 1 223 ARG 223 220 220 ARG ARG A . n 
A 1 224 GLU 224 221 221 GLU GLU A . n 
A 1 225 ALA 225 222 222 ALA ALA A . n 
A 1 226 LEU 226 223 223 LEU LEU A . n 
A 1 227 ARG 227 224 224 ARG ARG A . n 
A 1 228 GLU 228 225 225 GLU GLU A . n 
A 1 229 ALA 229 226 226 ALA ALA A . n 
A 1 230 ALA 230 227 227 ALA ALA A . n 
A 1 231 PRO 231 228 228 PRO PRO A . n 
A 1 232 ASP 232 229 229 ASP ASP A . n 
A 1 233 GLY 233 230 230 GLY GLY A . n 
A 1 234 VAL 234 231 231 VAL VAL A . n 
A 1 235 ASP 235 232 232 ASP ASP A . n 
A 1 236 LYS 236 233 233 LYS LYS A . n 
A 1 237 TYR 237 234 234 TYR TYR A . n 
A 1 238 PHE 238 235 235 PHE PHE A . n 
A 1 239 ASP 239 236 236 ASP ASP A . n 
A 1 240 SER 240 237 237 SER SER A . n 
A 1 241 ILE 241 238 238 ILE ILE A . n 
A 1 242 GLY 242 239 239 GLY GLY A . n 
A 1 243 GLY 243 240 240 GLY GLY A . n 
A 1 244 SER 244 241 241 SER SER A . n 
A 1 245 VAL 245 242 242 VAL VAL A . n 
A 1 246 THR 246 243 243 THR THR A . n 
A 1 247 ASP 247 244 244 ASP ASP A . n 
A 1 248 ALA 248 245 245 ALA ALA A . n 
A 1 249 VAL 249 246 246 VAL VAL A . n 
A 1 250 PHE 250 247 247 PHE PHE A . n 
A 1 251 SER 251 248 248 SER SER A . n 
A 1 252 MET 252 249 249 MET MET A . n 
A 1 253 LEU 253 250 250 LEU LEU A . n 
A 1 254 ASN 254 251 251 ASN ASN A . n 
A 1 255 VAL 255 252 252 VAL VAL A . n 
A 1 256 GLY 256 253 253 GLY GLY A . n 
A 1 257 SER 257 254 254 SER SER A . n 
A 1 258 GLN 258 255 255 GLN GLN A . n 
A 1 259 VAL 259 256 256 VAL VAL A . n 
A 1 260 ALA 260 257 257 ALA ALA A . n 
A 1 261 VAL 261 258 258 VAL VAL A . n 
A 1 262 CYS 262 259 259 CYS CYS A . n 
A 1 263 TRP 263 260 260 TRP TRP A . n 
A 1 264 GLN 264 261 261 GLN GLN A . n 
A 1 265 TRP 265 262 262 TRP TRP A . n 
A 1 266 ALA 266 263 263 ALA ALA A . n 
A 1 267 THR 267 264 264 THR THR A . n 
A 1 268 GLN 268 265 265 GLN GLN A . n 
A 1 269 VAL 269 266 266 VAL VAL A . n 
A 1 270 GLN 270 267 267 GLN GLN A . n 
A 1 271 ARG 271 268 268 ARG ARG A . n 
A 1 272 ASP 272 269 269 ASP ASP A . n 
A 1 273 TYR 273 270 270 TYR TYR A . n 
A 1 274 HIS 274 271 271 HIS HIS A . n 
A 1 275 GLY 275 272 272 GLY GLY A . n 
A 1 276 PRO 276 273 273 PRO PRO A . n 
A 1 277 ARG 277 274 274 ARG ARG A . n 
A 1 278 LEU 278 275 275 LEU LEU A . n 
A 1 279 LEU 279 276 276 LEU LEU A . n 
A 1 280 PRO 280 277 277 PRO PRO A . n 
A 1 281 TYR 281 278 278 TYR TYR A . n 
A 1 282 ILE 282 279 279 ILE ILE A . n 
A 1 283 MET 283 280 280 MET MET A . n 
A 1 284 PHE 284 281 281 PHE PHE A . n 
A 1 285 PRO 285 282 282 PRO PRO A . n 
A 1 286 ARG 286 283 283 ARG ARG A . n 
A 1 287 ALA 287 284 284 ALA ALA A . n 
A 1 288 THR 288 285 285 THR THR A . n 
A 1 289 ILE 289 286 286 ILE ILE A . n 
A 1 290 ARG 290 287 287 ARG ARG A . n 
A 1 291 GLY 291 288 288 GLY GLY A . n 
A 1 292 ILE 292 289 289 ILE ILE A . n 
A 1 293 PHE 293 290 290 PHE PHE A . n 
A 1 294 SER 294 291 291 SER SER A . n 
A 1 295 LEU 295 292 292 LEU LEU A . n 
A 1 296 GLU 296 293 293 GLU GLU A . n 
A 1 297 TRP 297 294 294 TRP TRP A . n 
A 1 298 PHE 298 295 295 PHE PHE A . n 
A 1 299 THR 299 296 296 THR THR A . n 
A 1 300 GLU 300 297 297 GLU GLU A . n 
A 1 301 GLN 301 298 298 GLN GLN A . n 
A 1 302 ASN 302 299 299 ASN ASN A . n 
A 1 303 TRP 303 300 300 TRP TRP A . n 
A 1 304 SER 304 301 301 SER SER A . n 
A 1 305 ALA 305 302 302 ALA ALA A . n 
A 1 306 LEU 306 303 303 LEU LEU A . n 
A 1 307 HIS 307 304 304 HIS HIS A . n 
A 1 308 GLU 308 305 305 GLU GLU A . n 
A 1 309 GLU 309 306 306 GLU GLU A . n 
A 1 310 LEU 310 307 307 LEU LEU A . n 
A 1 311 GLY 311 308 308 GLY GLY A . n 
A 1 312 GLY 312 309 309 GLY GLY A . n 
A 1 313 LEU 313 310 310 LEU LEU A . n 
A 1 314 VAL 314 311 311 VAL VAL A . n 
A 1 315 ARG 315 312 312 ARG ARG A . n 
A 1 316 ARG 316 313 313 ARG ARG A . n 
A 1 317 GLN 317 314 314 GLN GLN A . n 
A 1 318 GLU 318 315 315 GLU GLU A . n 
A 1 319 LEU 319 316 316 LEU LEU A . n 
A 1 320 VAL 320 317 317 VAL VAL A . n 
A 1 321 ALA 321 318 318 ALA ALA A . n 
A 1 322 HIS 322 319 319 HIS HIS A . n 
A 1 323 GLU 323 320 320 GLU GLU A . n 
A 1 324 THR 324 321 321 THR THR A . n 
A 1 325 VAL 325 322 322 VAL VAL A . n 
A 1 326 GLN 326 323 323 GLN GLN A . n 
A 1 327 ASP 327 324 324 ASP ASP A . n 
A 1 328 GLY 328 325 325 GLY GLY A . n 
A 1 329 PHE 329 326 326 PHE PHE A . n 
A 1 330 GLU 330 327 327 GLU GLU A . n 
A 1 331 HIS 331 328 328 HIS HIS A . n 
A 1 332 ILE 332 329 329 ILE ILE A . n 
A 1 333 PRO 333 330 330 PRO PRO A . n 
A 1 334 ALA 334 331 331 ALA ALA A . n 
A 1 335 ALA 335 332 332 ALA ALA A . n 
A 1 336 TYR 336 333 333 TYR TYR A . n 
A 1 337 GLN 337 334 334 GLN GLN A . n 
A 1 338 THR 338 335 335 THR THR A . n 
A 1 339 LEU 339 336 336 LEU LEU A . n 
A 1 340 PHE 340 337 337 PHE PHE A . n 
A 1 341 SER 341 338 338 SER SER A . n 
A 1 342 ALA 342 339 339 ALA ALA A . n 
A 1 343 SER 343 340 340 SER SER A . n 
A 1 344 GLU 344 341 341 GLU GLU A . n 
A 1 345 SER 345 342 342 SER SER A . n 
A 1 346 ASN 346 343 343 ASN ASN A . n 
A 1 347 ARG 347 344 344 ARG ARG A . n 
A 1 348 GLY 348 345 345 GLY GLY A . n 
A 1 349 LYS 349 346 346 LYS LYS A . n 
A 1 350 VAL 350 347 347 VAL VAL A . n 
A 1 351 LEU 351 348 348 LEU LEU A . n 
A 1 352 VAL 352 349 349 VAL VAL A . n 
A 1 353 ARG 353 350 350 ARG ARG A . n 
A 1 354 VAL 354 351 351 VAL VAL A . n 
B 1 1   LEU 1   -2  -2  LEU LEU B . n 
B 1 2   GLY 2   -1  -1  GLY GLY B . n 
B 1 3   SER 3   0   0   SER SER B . n 
B 1 4   MET 4   1   1   MET MET B . n 
B 1 5   LYS 5   2   2   LYS LYS B . n 
B 1 6   THR 6   3   3   THR THR B . n 
B 1 7   GLU 7   4   4   GLU GLU B . n 
B 1 8   ARG 8   5   5   ARG ARG B . n 
B 1 9   TRP 9   6   6   TRP TRP B . n 
B 1 10  VAL 10  7   7   VAL VAL B . n 
B 1 11  VAL 11  8   8   VAL VAL B . n 
B 1 12  ARG 12  9   9   ARG ARG B . n 
B 1 13  GLU 13  10  10  GLU GLU B . n 
B 1 14  HIS 14  11  11  HIS HIS B . n 
B 1 15  VAL 15  12  12  VAL VAL B . n 
B 1 16  GLU 16  13  13  GLU GLU B . n 
B 1 17  GLY 17  14  14  GLY GLY B . n 
B 1 18  VAL 18  15  15  VAL VAL B . n 
B 1 19  PRO 19  16  16  PRO PRO B . n 
B 1 20  ASP 20  17  17  ASP ASP B . n 
B 1 21  ALA 21  18  18  ALA ALA B . n 
B 1 22  ALA 22  19  19  ALA ALA B . n 
B 1 23  ARG 23  20  20  ARG ARG B . n 
B 1 24  ILE 24  21  21  ILE ILE B . n 
B 1 25  TYR 25  22  22  TYR TYR B . n 
B 1 26  GLU 26  23  23  GLU GLU B . n 
B 1 27  LYS 27  24  24  LYS LYS B . n 
B 1 28  VAL 28  25  25  VAL VAL B . n 
B 1 29  GLU 29  26  26  GLU GLU B . n 
B 1 30  THR 30  27  27  THR THR B . n 
B 1 31  GLU 31  28  28  GLU GLU B . n 
B 1 32  LEU 32  29  29  LEU LEU B . n 
B 1 33  ASN 33  30  30  ASN ASN B . n 
B 1 34  THR 34  31  31  THR THR B . n 
B 1 35  ARG 35  32  32  ARG ARG B . n 
B 1 36  LEU 36  33  33  LEU LEU B . n 
B 1 37  GLY 37  34  34  GLY GLY B . n 
B 1 38  GLU 38  35  35  GLU GLU B . n 
B 1 39  GLU 39  36  36  GLU GLU B . n 
B 1 40  GLN 40  37  37  GLN GLN B . n 
B 1 41  MET 41  38  38  MET MET B . n 
B 1 42  LEU 42  39  39  LEU LEU B . n 
B 1 43  LEU 43  40  40  LEU LEU B . n 
B 1 44  LYS 44  41  41  LYS LYS B . n 
B 1 45  THR 45  42  42  THR THR B . n 
B 1 46  LEU 46  43  43  LEU LEU B . n 
B 1 47  TYR 47  44  44  TYR TYR B . n 
B 1 48  VAL 48  45  45  VAL VAL B . n 
B 1 49  SER 49  46  46  SER SER B . n 
B 1 50  VAL 50  47  47  VAL VAL B . n 
B 1 51  ASP 51  48  48  ASP ASP B . n 
B 1 52  PRO 52  49  49  PRO PRO B . n 
B 1 53  TYR 53  50  50  TYR TYR B . n 
B 1 54  LEU 54  51  51  LEU LEU B . n 
B 1 55  GLN 55  52  52  GLN GLN B . n 
B 1 56  GLY 56  53  53  GLY GLY B . n 
B 1 57  ILE 57  54  54  ILE ILE B . n 
B 1 58  CYS 58  55  55  CYS CYS B . n 
B 1 59  LEU 59  56  56  LEU LEU B . n 
B 1 60  ASP 60  57  57  ASP ASP B . n 
B 1 61  THR 61  58  58  THR THR B . n 
B 1 62  PRO 62  59  59  PRO PRO B . n 
B 1 63  ILE 63  60  60  ILE ILE B . n 
B 1 64  GLY 64  61  61  GLY GLY B . n 
B 1 65  ASP 65  62  62  ASP ASP B . n 
B 1 66  HIS 66  63  63  HIS HIS B . n 
B 1 67  MET 67  64  64  MET MET B . n 
B 1 68  GLY 68  65  65  GLY GLY B . n 
B 1 69  ALA 69  66  66  ALA ALA B . n 
B 1 70  ASP 70  67  67  ASP ASP B . n 
B 1 71  SER 71  68  68  SER SER B . n 
B 1 72  ILE 72  69  69  ILE ILE B . n 
B 1 73  MET 73  70  70  MET MET B . n 
B 1 74  GLN 74  71  71  GLN GLN B . n 
B 1 75  VAL 75  72  72  VAL VAL B . n 
B 1 76  LEU 76  73  73  LEU LEU B . n 
B 1 77  ASP 77  74  74  ASP ASP B . n 
B 1 78  ALA 78  75  75  ALA ALA B . n 
B 1 79  GLY 79  76  76  GLY GLY B . n 
B 1 80  PRO 80  77  77  PRO PRO B . n 
B 1 81  ASN 81  78  78  ASN ASN B . n 
B 1 82  ALA 82  79  79  ALA ALA B . n 
B 1 83  PRO 83  80  80  PRO PRO B . n 
B 1 84  PHE 84  81  81  PHE PHE B . n 
B 1 85  ARG 85  82  82  ARG ARG B . n 
B 1 86  PRO 86  83  83  PRO PRO B . n 
B 1 87  GLY 87  84  84  GLY GLY B . n 
B 1 88  ASP 88  85  85  ASP ASP B . n 
B 1 89  LEU 89  86  86  LEU LEU B . n 
B 1 90  VAL 90  87  87  VAL VAL B . n 
B 1 91  GLN 91  88  88  GLN GLN B . n 
B 1 92  GLY 92  89  89  GLY GLY B . n 
B 1 93  PHE 93  90  90  PHE PHE B . n 
B 1 94  GLY 94  91  91  GLY GLY B . n 
B 1 95  GLY 95  92  92  GLY GLY B . n 
B 1 96  TRP 96  93  93  TRP TRP B . n 
B 1 97  ARG 97  94  94  ARG ARG B . n 
B 1 98  THR 98  95  95  THR THR B . n 
B 1 99  HIS 99  96  96  HIS HIS B . n 
B 1 100 LEU 100 97  97  LEU LEU B . n 
B 1 101 VAL 101 98  98  VAL VAL B . n 
B 1 102 SER 102 99  99  SER SER B . n 
B 1 103 ASP 103 100 100 ASP ASP B . n 
B 1 104 GLY 104 101 101 GLY GLY B . n 
B 1 105 LYS 105 102 102 LYS LYS B . n 
B 1 106 PRO 106 103 103 PRO PRO B . n 
B 1 107 LYS 107 104 104 LYS LYS B . n 
B 1 108 LEU 108 105 105 LEU LEU B . n 
B 1 109 TRP 109 106 106 TRP TRP B . n 
B 1 110 GLN 110 107 107 GLN GLN B . n 
B 1 111 THR 111 108 108 THR THR B . n 
B 1 112 GLY 112 109 109 GLY GLY B . n 
B 1 113 THR 113 110 110 THR THR B . n 
B 1 114 PHE 114 111 111 PHE PHE B . n 
B 1 115 PRO 115 112 112 PRO PRO B . n 
B 1 116 MET 116 113 113 MET MET B . n 
B 1 117 VAL 117 114 114 VAL VAL B . n 
B 1 118 PHE 118 115 115 PHE PHE B . n 
B 1 119 PRO 119 116 116 PRO PRO B . n 
B 1 120 ALA 120 117 117 ALA ALA B . n 
B 1 121 TYR 121 118 118 TYR TYR B . n 
B 1 122 ARG 122 119 119 ARG ARG B . n 
B 1 123 LYS 123 120 120 LYS LYS B . n 
B 1 124 LEU 124 121 121 LEU LEU B . n 
B 1 125 ASP 125 122 122 ASP ASP B . n 
B 1 126 LEU 126 123 123 LEU LEU B . n 
B 1 127 ARG 127 124 124 ARG ARG B . n 
B 1 128 HIS 128 125 125 HIS HIS B . n 
B 1 129 TYR 129 126 126 TYR TYR B . n 
B 1 130 ASP 130 127 127 ASP ASP B . n 
B 1 131 ASP 131 128 128 ASP ASP B . n 
B 1 132 ALA 132 129 129 ALA ALA B . n 
B 1 133 LEU 133 130 130 LEU LEU B . n 
B 1 134 PRO 134 131 131 PRO PRO B . n 
B 1 135 LEU 135 132 132 LEU LEU B . n 
B 1 136 SER 136 133 133 SER SER B . n 
B 1 137 THR 137 134 134 THR THR B . n 
B 1 138 ALA 138 135 135 ALA ALA B . n 
B 1 139 LEU 139 136 136 LEU LEU B . n 
B 1 140 GLY 140 137 137 GLY GLY B . n 
B 1 141 VAL 141 138 138 VAL VAL B . n 
B 1 142 MET 142 139 139 MET MET B . n 
B 1 143 GLY 143 140 140 GLY GLY B . n 
B 1 144 GLY 144 141 141 GLY GLY B . n 
B 1 145 PRO 145 142 142 PRO PRO B . n 
B 1 146 GLY 146 143 143 GLY GLY B . n 
B 1 147 MET 147 144 144 MET MET B . n 
B 1 148 THR 148 145 145 THR THR B . n 
B 1 149 ALA 149 146 146 ALA ALA B . n 
B 1 150 TRP 150 147 147 TRP TRP B . n 
B 1 151 GLY 151 148 148 GLY GLY B . n 
B 1 152 THR 152 149 149 THR THR B . n 
B 1 153 MET 153 150 150 MET MET B . n 
B 1 154 THR 154 151 151 THR THR B . n 
B 1 155 LYS 155 152 152 LYS LYS B . n 
B 1 156 PHE 156 153 153 PHE PHE B . n 
B 1 157 MET 157 154 154 MET MET B . n 
B 1 158 GLN 158 155 155 GLN GLN B . n 
B 1 159 VAL 159 156 156 VAL VAL B . n 
B 1 160 ARG 160 157 157 ARG ARG B . n 
B 1 161 PRO 161 158 158 PRO PRO B . n 
B 1 162 GLY 162 159 159 GLY GLY B . n 
B 1 163 ASP 163 160 160 ASP ASP B . n 
B 1 164 THR 164 161 161 THR THR B . n 
B 1 165 VAL 165 162 162 VAL VAL B . n 
B 1 166 VAL 166 163 163 VAL VAL B . n 
B 1 167 VAL 167 164 164 VAL VAL B . n 
B 1 168 SER 168 165 165 SER SER B . n 
B 1 169 GLY 169 166 166 GLY GLY B . n 
B 1 170 ALA 170 167 167 ALA ALA B . n 
B 1 171 SER 171 168 168 SER SER B . n 
B 1 172 GLY 172 169 169 GLY GLY B . n 
B 1 173 MET 173 170 170 MET MET B . n 
B 1 174 ILE 174 171 171 ILE ILE B . n 
B 1 175 GLY 175 172 172 GLY GLY B . n 
B 1 176 THR 176 173 173 THR THR B . n 
B 1 177 LEU 177 174 174 LEU LEU B . n 
B 1 178 VAL 178 175 175 VAL VAL B . n 
B 1 179 GLY 179 176 176 GLY GLY B . n 
B 1 180 GLN 180 177 177 GLN GLN B . n 
B 1 181 MET 181 178 178 MET MET B . n 
B 1 182 ALA 182 179 179 ALA ALA B . n 
B 1 183 LYS 183 180 180 LYS LYS B . n 
B 1 184 ARG 184 181 181 ARG ARG B . n 
B 1 185 ALA 185 182 182 ALA ALA B . n 
B 1 186 GLY 186 183 183 GLY GLY B . n 
B 1 187 ALA 187 184 184 ALA ALA B . n 
B 1 188 ARG 188 185 185 ARG ARG B . n 
B 1 189 VAL 189 186 186 VAL VAL B . n 
B 1 190 VAL 190 187 187 VAL VAL B . n 
B 1 191 GLY 191 188 188 GLY GLY B . n 
B 1 192 THR 192 189 189 THR THR B . n 
B 1 193 ALA 193 190 190 ALA ALA B . n 
B 1 194 GLY 194 191 191 GLY GLY B . n 
B 1 195 SER 195 192 192 SER SER B . n 
B 1 196 ALA 196 193 193 ALA ALA B . n 
B 1 197 GLY 197 194 194 GLY GLY B . n 
B 1 198 LYS 198 195 195 LYS LYS B . n 
B 1 199 ALA 199 196 196 ALA ALA B . n 
B 1 200 ARG 200 197 197 ARG ARG B . n 
B 1 201 TYR 201 198 198 TYR TYR B . n 
B 1 202 LEU 202 199 199 LEU LEU B . n 
B 1 203 SER 203 200 200 SER SER B . n 
B 1 204 GLN 204 201 201 GLN GLN B . n 
B 1 205 LEU 205 202 202 LEU LEU B . n 
B 1 206 GLY 206 203 203 GLY GLY B . n 
B 1 207 PHE 207 204 204 PHE PHE B . n 
B 1 208 ASP 208 205 205 ASP ASP B . n 
B 1 209 ALA 209 206 206 ALA ALA B . n 
B 1 210 VAL 210 207 207 VAL VAL B . n 
B 1 211 ILE 211 208 208 ILE ILE B . n 
B 1 212 ASP 212 209 209 ASP ASP B . n 
B 1 213 TYR 213 210 210 TYR TYR B . n 
B 1 214 LYS 214 211 211 LYS LYS B . n 
B 1 215 LEU 215 212 212 LEU LEU B . n 
B 1 216 ALA 216 213 213 ALA ALA B . n 
B 1 217 ASP 217 214 214 ASP ASP B . n 
B 1 218 ASP 218 215 215 ASP ASP B . n 
B 1 219 ALA 219 216 216 ALA ALA B . n 
B 1 220 ASP 220 217 217 ASP ASP B . n 
B 1 221 LYS 221 218 218 LYS LYS B . n 
B 1 222 MET 222 219 219 MET MET B . n 
B 1 223 ARG 223 220 220 ARG ARG B . n 
B 1 224 GLU 224 221 221 GLU GLU B . n 
B 1 225 ALA 225 222 222 ALA ALA B . n 
B 1 226 LEU 226 223 223 LEU LEU B . n 
B 1 227 ARG 227 224 224 ARG ARG B . n 
B 1 228 GLU 228 225 225 GLU GLU B . n 
B 1 229 ALA 229 226 226 ALA ALA B . n 
B 1 230 ALA 230 227 227 ALA ALA B . n 
B 1 231 PRO 231 228 228 PRO PRO B . n 
B 1 232 ASP 232 229 229 ASP ASP B . n 
B 1 233 GLY 233 230 230 GLY GLY B . n 
B 1 234 VAL 234 231 231 VAL VAL B . n 
B 1 235 ASP 235 232 232 ASP ASP B . n 
B 1 236 LYS 236 233 233 LYS LYS B . n 
B 1 237 TYR 237 234 234 TYR TYR B . n 
B 1 238 PHE 238 235 235 PHE PHE B . n 
B 1 239 ASP 239 236 236 ASP ASP B . n 
B 1 240 SER 240 237 237 SER SER B . n 
B 1 241 ILE 241 238 238 ILE ILE B . n 
B 1 242 GLY 242 239 239 GLY GLY B . n 
B 1 243 GLY 243 240 240 GLY GLY B . n 
B 1 244 SER 244 241 241 SER SER B . n 
B 1 245 VAL 245 242 242 VAL VAL B . n 
B 1 246 THR 246 243 243 THR THR B . n 
B 1 247 ASP 247 244 244 ASP ASP B . n 
B 1 248 ALA 248 245 245 ALA ALA B . n 
B 1 249 VAL 249 246 246 VAL VAL B . n 
B 1 250 PHE 250 247 247 PHE PHE B . n 
B 1 251 SER 251 248 248 SER SER B . n 
B 1 252 MET 252 249 249 MET MET B . n 
B 1 253 LEU 253 250 250 LEU LEU B . n 
B 1 254 ASN 254 251 251 ASN ASN B . n 
B 1 255 VAL 255 252 252 VAL VAL B . n 
B 1 256 GLY 256 253 253 GLY GLY B . n 
B 1 257 SER 257 254 254 SER SER B . n 
B 1 258 GLN 258 255 255 GLN GLN B . n 
B 1 259 VAL 259 256 256 VAL VAL B . n 
B 1 260 ALA 260 257 257 ALA ALA B . n 
B 1 261 VAL 261 258 258 VAL VAL B . n 
B 1 262 CYS 262 259 259 CYS CYS B . n 
B 1 263 TRP 263 260 260 TRP TRP B . n 
B 1 264 GLN 264 261 261 GLN GLN B . n 
B 1 265 TRP 265 262 262 TRP TRP B . n 
B 1 266 ALA 266 263 263 ALA ALA B . n 
B 1 267 THR 267 264 264 THR THR B . n 
B 1 268 GLN 268 265 265 GLN GLN B . n 
B 1 269 VAL 269 266 266 VAL VAL B . n 
B 1 270 GLN 270 267 267 GLN GLN B . n 
B 1 271 ARG 271 268 268 ARG ARG B . n 
B 1 272 ASP 272 269 269 ASP ASP B . n 
B 1 273 TYR 273 270 270 TYR TYR B . n 
B 1 274 HIS 274 271 271 HIS HIS B . n 
B 1 275 GLY 275 272 272 GLY GLY B . n 
B 1 276 PRO 276 273 273 PRO PRO B . n 
B 1 277 ARG 277 274 274 ARG ARG B . n 
B 1 278 LEU 278 275 275 LEU LEU B . n 
B 1 279 LEU 279 276 276 LEU LEU B . n 
B 1 280 PRO 280 277 277 PRO PRO B . n 
B 1 281 TYR 281 278 278 TYR TYR B . n 
B 1 282 ILE 282 279 279 ILE ILE B . n 
B 1 283 MET 283 280 280 MET MET B . n 
B 1 284 PHE 284 281 281 PHE PHE B . n 
B 1 285 PRO 285 282 282 PRO PRO B . n 
B 1 286 ARG 286 283 283 ARG ARG B . n 
B 1 287 ALA 287 284 284 ALA ALA B . n 
B 1 288 THR 288 285 285 THR THR B . n 
B 1 289 ILE 289 286 286 ILE ILE B . n 
B 1 290 ARG 290 287 287 ARG ARG B . n 
B 1 291 GLY 291 288 288 GLY GLY B . n 
B 1 292 ILE 292 289 289 ILE ILE B . n 
B 1 293 PHE 293 290 290 PHE PHE B . n 
B 1 294 SER 294 291 291 SER SER B . n 
B 1 295 LEU 295 292 292 LEU LEU B . n 
B 1 296 GLU 296 293 293 GLU GLU B . n 
B 1 297 TRP 297 294 294 TRP TRP B . n 
B 1 298 PHE 298 295 295 PHE PHE B . n 
B 1 299 THR 299 296 296 THR THR B . n 
B 1 300 GLU 300 297 297 GLU GLU B . n 
B 1 301 GLN 301 298 298 GLN GLN B . n 
B 1 302 ASN 302 299 299 ASN ASN B . n 
B 1 303 TRP 303 300 300 TRP TRP B . n 
B 1 304 SER 304 301 301 SER SER B . n 
B 1 305 ALA 305 302 302 ALA ALA B . n 
B 1 306 LEU 306 303 303 LEU LEU B . n 
B 1 307 HIS 307 304 304 HIS HIS B . n 
B 1 308 GLU 308 305 305 GLU GLU B . n 
B 1 309 GLU 309 306 306 GLU GLU B . n 
B 1 310 LEU 310 307 307 LEU LEU B . n 
B 1 311 GLY 311 308 308 GLY GLY B . n 
B 1 312 GLY 312 309 309 GLY GLY B . n 
B 1 313 LEU 313 310 310 LEU LEU B . n 
B 1 314 VAL 314 311 311 VAL VAL B . n 
B 1 315 ARG 315 312 312 ARG ARG B . n 
B 1 316 ARG 316 313 313 ARG ARG B . n 
B 1 317 GLN 317 314 314 GLN GLN B . n 
B 1 318 GLU 318 315 315 GLU GLU B . n 
B 1 319 LEU 319 316 316 LEU LEU B . n 
B 1 320 VAL 320 317 317 VAL VAL B . n 
B 1 321 ALA 321 318 318 ALA ALA B . n 
B 1 322 HIS 322 319 319 HIS HIS B . n 
B 1 323 GLU 323 320 320 GLU GLU B . n 
B 1 324 THR 324 321 321 THR THR B . n 
B 1 325 VAL 325 322 322 VAL VAL B . n 
B 1 326 GLN 326 323 323 GLN GLN B . n 
B 1 327 ASP 327 324 324 ASP ASP B . n 
B 1 328 GLY 328 325 325 GLY GLY B . n 
B 1 329 PHE 329 326 326 PHE PHE B . n 
B 1 330 GLU 330 327 327 GLU GLU B . n 
B 1 331 HIS 331 328 328 HIS HIS B . n 
B 1 332 ILE 332 329 329 ILE ILE B . n 
B 1 333 PRO 333 330 330 PRO PRO B . n 
B 1 334 ALA 334 331 331 ALA ALA B . n 
B 1 335 ALA 335 332 332 ALA ALA B . n 
B 1 336 TYR 336 333 333 TYR TYR B . n 
B 1 337 GLN 337 334 334 GLN GLN B . n 
B 1 338 THR 338 335 335 THR THR B . n 
B 1 339 LEU 339 336 336 LEU LEU B . n 
B 1 340 PHE 340 337 337 PHE PHE B . n 
B 1 341 SER 341 338 338 SER SER B . n 
B 1 342 ALA 342 339 339 ALA ALA B . n 
B 1 343 SER 343 340 340 SER SER B . n 
B 1 344 GLU 344 341 341 GLU GLU B . n 
B 1 345 SER 345 342 342 SER SER B . n 
B 1 346 ASN 346 343 343 ASN ASN B . n 
B 1 347 ARG 347 344 344 ARG ARG B . n 
B 1 348 GLY 348 345 345 GLY GLY B . n 
B 1 349 LYS 349 346 346 LYS LYS B . n 
B 1 350 VAL 350 347 347 VAL VAL B . n 
B 1 351 LEU 351 348 348 LEU LEU B . n 
B 1 352 VAL 352 349 349 VAL VAL B . n 
B 1 353 ARG 353 350 350 ARG ARG B . n 
B 1 354 VAL 354 351 351 VAL VAL B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1EBZ ? ? A1EBZ ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAP   ? ? NAP   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1EBZ 1  401 502 A1EBZ ATB A . 
D 3 NAP   1  402 501 NAP   NAP A . 
E 2 A1EBZ 1  401 502 A1EBZ ATB B . 
F 3 NAP   1  402 501 NAP   NAP B . 
G 4 HOH   1  501 48  HOH   HOH A . 
G 4 HOH   2  502 32  HOH   HOH A . 
G 4 HOH   3  503 96  HOH   HOH A . 
G 4 HOH   4  504 38  HOH   HOH A . 
G 4 HOH   5  505 104 HOH   HOH A . 
G 4 HOH   6  506 134 HOH   HOH A . 
G 4 HOH   7  507 14  HOH   HOH A . 
G 4 HOH   8  508 73  HOH   HOH A . 
G 4 HOH   9  509 44  HOH   HOH A . 
G 4 HOH   10 510 18  HOH   HOH A . 
G 4 HOH   11 511 16  HOH   HOH A . 
G 4 HOH   12 512 83  HOH   HOH A . 
G 4 HOH   13 513 65  HOH   HOH A . 
G 4 HOH   14 514 36  HOH   HOH A . 
G 4 HOH   15 515 70  HOH   HOH A . 
G 4 HOH   16 516 1   HOH   HOH A . 
G 4 HOH   17 517 67  HOH   HOH A . 
G 4 HOH   18 518 20  HOH   HOH A . 
G 4 HOH   19 519 68  HOH   HOH A . 
G 4 HOH   20 520 113 HOH   HOH A . 
G 4 HOH   21 521 57  HOH   HOH A . 
G 4 HOH   22 522 85  HOH   HOH A . 
G 4 HOH   23 523 124 HOH   HOH A . 
G 4 HOH   24 524 61  HOH   HOH A . 
G 4 HOH   25 525 58  HOH   HOH A . 
G 4 HOH   26 526 15  HOH   HOH A . 
G 4 HOH   27 527 9   HOH   HOH A . 
G 4 HOH   28 528 34  HOH   HOH A . 
G 4 HOH   29 529 98  HOH   HOH A . 
G 4 HOH   30 530 12  HOH   HOH A . 
G 4 HOH   31 531 55  HOH   HOH A . 
G 4 HOH   32 532 2   HOH   HOH A . 
G 4 HOH   33 533 43  HOH   HOH A . 
G 4 HOH   34 534 35  HOH   HOH A . 
G 4 HOH   35 535 4   HOH   HOH A . 
G 4 HOH   36 536 72  HOH   HOH A . 
G 4 HOH   37 537 60  HOH   HOH A . 
G 4 HOH   38 538 40  HOH   HOH A . 
G 4 HOH   39 539 97  HOH   HOH A . 
G 4 HOH   40 540 7   HOH   HOH A . 
G 4 HOH   41 541 13  HOH   HOH A . 
G 4 HOH   42 542 31  HOH   HOH A . 
G 4 HOH   43 543 84  HOH   HOH A . 
G 4 HOH   44 544 26  HOH   HOH A . 
G 4 HOH   45 545 116 HOH   HOH A . 
G 4 HOH   46 546 132 HOH   HOH A . 
G 4 HOH   47 547 46  HOH   HOH A . 
G 4 HOH   48 548 75  HOH   HOH A . 
G 4 HOH   49 549 129 HOH   HOH A . 
G 4 HOH   50 550 66  HOH   HOH A . 
G 4 HOH   51 551 120 HOH   HOH A . 
G 4 HOH   52 552 95  HOH   HOH A . 
G 4 HOH   53 553 64  HOH   HOH A . 
G 4 HOH   54 554 138 HOH   HOH A . 
G 4 HOH   55 555 39  HOH   HOH A . 
G 4 HOH   56 556 102 HOH   HOH A . 
G 4 HOH   57 557 25  HOH   HOH A . 
G 4 HOH   58 558 141 HOH   HOH A . 
G 4 HOH   59 559 76  HOH   HOH A . 
G 4 HOH   60 560 123 HOH   HOH A . 
G 4 HOH   61 561 137 HOH   HOH A . 
G 4 HOH   62 562 130 HOH   HOH A . 
G 4 HOH   63 563 77  HOH   HOH A . 
G 4 HOH   64 564 118 HOH   HOH A . 
G 4 HOH   65 565 119 HOH   HOH A . 
G 4 HOH   66 566 74  HOH   HOH A . 
G 4 HOH   67 567 90  HOH   HOH A . 
G 4 HOH   68 568 143 HOH   HOH A . 
G 4 HOH   69 569 127 HOH   HOH A . 
G 4 HOH   70 570 110 HOH   HOH A . 
G 4 HOH   71 571 142 HOH   HOH A . 
G 4 HOH   72 572 115 HOH   HOH A . 
G 4 HOH   73 573 140 HOH   HOH A . 
G 4 HOH   74 574 150 HOH   HOH A . 
G 4 HOH   75 575 117 HOH   HOH A . 
H 4 HOH   1  501 71  HOH   HOH B . 
H 4 HOH   2  502 17  HOH   HOH B . 
H 4 HOH   3  503 121 HOH   HOH B . 
H 4 HOH   4  504 136 HOH   HOH B . 
H 4 HOH   5  505 22  HOH   HOH B . 
H 4 HOH   6  506 112 HOH   HOH B . 
H 4 HOH   7  507 3   HOH   HOH B . 
H 4 HOH   8  508 50  HOH   HOH B . 
H 4 HOH   9  509 131 HOH   HOH B . 
H 4 HOH   10 510 11  HOH   HOH B . 
H 4 HOH   11 511 105 HOH   HOH B . 
H 4 HOH   12 512 114 HOH   HOH B . 
H 4 HOH   13 513 24  HOH   HOH B . 
H 4 HOH   14 514 62  HOH   HOH B . 
H 4 HOH   15 515 69  HOH   HOH B . 
H 4 HOH   16 516 30  HOH   HOH B . 
H 4 HOH   17 517 21  HOH   HOH B . 
H 4 HOH   18 518 5   HOH   HOH B . 
H 4 HOH   19 519 10  HOH   HOH B . 
H 4 HOH   20 520 27  HOH   HOH B . 
H 4 HOH   21 521 63  HOH   HOH B . 
H 4 HOH   22 522 28  HOH   HOH B . 
H 4 HOH   23 523 45  HOH   HOH B . 
H 4 HOH   24 524 99  HOH   HOH B . 
H 4 HOH   25 525 41  HOH   HOH B . 
H 4 HOH   26 526 78  HOH   HOH B . 
H 4 HOH   27 527 125 HOH   HOH B . 
H 4 HOH   28 528 106 HOH   HOH B . 
H 4 HOH   29 529 6   HOH   HOH B . 
H 4 HOH   30 530 103 HOH   HOH B . 
H 4 HOH   31 531 59  HOH   HOH B . 
H 4 HOH   32 532 53  HOH   HOH B . 
H 4 HOH   33 533 51  HOH   HOH B . 
H 4 HOH   34 534 37  HOH   HOH B . 
H 4 HOH   35 535 8   HOH   HOH B . 
H 4 HOH   36 536 42  HOH   HOH B . 
H 4 HOH   37 537 23  HOH   HOH B . 
H 4 HOH   38 538 49  HOH   HOH B . 
H 4 HOH   39 539 93  HOH   HOH B . 
H 4 HOH   40 540 107 HOH   HOH B . 
H 4 HOH   41 541 92  HOH   HOH B . 
H 4 HOH   42 542 56  HOH   HOH B . 
H 4 HOH   43 543 52  HOH   HOH B . 
H 4 HOH   44 544 87  HOH   HOH B . 
H 4 HOH   45 545 82  HOH   HOH B . 
H 4 HOH   46 546 86  HOH   HOH B . 
H 4 HOH   47 547 80  HOH   HOH B . 
H 4 HOH   48 548 88  HOH   HOH B . 
H 4 HOH   49 549 19  HOH   HOH B . 
H 4 HOH   50 550 89  HOH   HOH B . 
H 4 HOH   51 551 94  HOH   HOH B . 
H 4 HOH   52 552 108 HOH   HOH B . 
H 4 HOH   53 553 33  HOH   HOH B . 
H 4 HOH   54 554 54  HOH   HOH B . 
H 4 HOH   55 555 47  HOH   HOH B . 
H 4 HOH   56 556 133 HOH   HOH B . 
H 4 HOH   57 557 29  HOH   HOH B . 
H 4 HOH   58 558 91  HOH   HOH B . 
H 4 HOH   59 559 149 HOH   HOH B . 
H 4 HOH   60 560 101 HOH   HOH B . 
H 4 HOH   61 561 81  HOH   HOH B . 
H 4 HOH   62 562 135 HOH   HOH B . 
H 4 HOH   63 563 128 HOH   HOH B . 
H 4 HOH   64 564 144 HOH   HOH B . 
H 4 HOH   65 565 122 HOH   HOH B . 
H 4 HOH   66 566 79  HOH   HOH B . 
H 4 HOH   67 567 145 HOH   HOH B . 
H 4 HOH   68 568 126 HOH   HOH B . 
H 4 HOH   69 569 148 HOH   HOH B . 
H 4 HOH   70 570 139 HOH   HOH B . 
H 4 HOH   71 571 100 HOH   HOH B . 
H 4 HOH   72 572 109 HOH   HOH B . 
H 4 HOH   73 573 147 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(???)' 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .       2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? .       3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .       4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? .       5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JI7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     87.275 
_cell.length_a_esd                 ? 
_cell.length_b                     87.275 
_cell.length_b_esd                 ? 
_cell.length_c                     226.042 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JI7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JI7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.76 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.49 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;PEG3350,sodium chloride,bis-tris
hydrochloride
;
_exptl_crystal_grow.pdbx_pH_range   8.5-9.0 
_exptl_crystal_grow.temp            277.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-07-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    Si111 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97915 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97915 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JI7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.53 
_reflns.d_resolution_low                               81.42 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     30090 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.17 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.53 
_reflns_shell.d_res_low                                     2.67 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4285 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.811 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JI7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.53 
_refine.ls_d_res_low                             59.53 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     29999 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 6.67 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1959 
_refine.ls_R_factor_R_free                       0.2438 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1925 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.00 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.53 
_refine_hist.d_res_low                        59.53 
_refine_hist.number_atoms_solvent             148 
_refine_hist.number_atoms_total               5788 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        5568 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 5782 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.969  ? 7866 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 19.230 ? 2232 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 858  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1004 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.53 2.60  . . 139 1941 100.00 . . . . 0.2680 . . . . . . . . . . . 0.3609 
'X-RAY DIFFRACTION' 2.60 2.67  . . 139 1963 100.00 . . . . 0.2523 . . . . . . . . . . . 0.3381 
'X-RAY DIFFRACTION' 2.67 2.74  . . 142 1979 100.00 . . . . 0.2428 . . . . . . . . . . . 0.2588 
'X-RAY DIFFRACTION' 2.74 2.83  . . 139 1952 100.00 . . . . 0.2361 . . . . . . . . . . . 0.2913 
'X-RAY DIFFRACTION' 2.83 2.93  . . 140 1953 100.00 . . . . 0.2194 . . . . . . . . . . . 0.2769 
'X-RAY DIFFRACTION' 2.93 3.05  . . 141 1975 100.00 . . . . 0.2397 . . . . . . . . . . . 0.2947 
'X-RAY DIFFRACTION' 3.05 3.19  . . 140 1965 100.00 . . . . 0.2393 . . . . . . . . . . . 0.3122 
'X-RAY DIFFRACTION' 3.19 3.36  . . 143 2001 100.00 . . . . 0.2156 . . . . . . . . . . . 0.2831 
'X-RAY DIFFRACTION' 3.36 3.57  . . 141 1971 100.00 . . . . 0.2022 . . . . . . . . . . . 0.2460 
'X-RAY DIFFRACTION' 3.57 3.84  . . 143 2005 100.00 . . . . 0.1903 . . . . . . . . . . . 0.2586 
'X-RAY DIFFRACTION' 3.85 4.23  . . 143 1999 100.00 . . . . 0.1643 . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 4.23 4.84  . . 145 2045 100.00 . . . . 0.1434 . . . . . . . . . . . 0.1683 
'X-RAY DIFFRACTION' 4.84 6.10  . . 147 2057 100.00 . . . . 0.1700 . . . . . . . . . . . 0.2430 
'X-RAY DIFFRACTION' 6.10 59.53 . . 158 2193 100.00 . . . . 0.1721 . . . . . . . . . . . 0.2177 
# 
_struct.entry_id                     9JI7 
_struct.title                        'NADP-dependent oxidoreductase complexed with NADP and substrate 2' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9JI7 
_struct_keywords.text            'alcohol dehydrogenase, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    C3PTT2_LYSEN 
_struct_ref.pdbx_db_accession          C3PTT2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKTERWVVREHVEGVPDAARIYEKVETELNTRLGEEQMLLKTLYVSVDPYLQGICLDTPIGDHMGADSIMQVLDAGPNAP
FRPGDLVQGFGGWRTHLVSDGKPKLWQTGTFPMVFPAYRKLDLRHYDDALPLSTALGVMGGPGMTAWGTMTKFMQVRPGD
TVVVSGASGMIGTLVGQMAKRAGARVVGTAGSAGKARYLSQLGFDAVIDYKLADDADKMREALREAAPDGVDKYFDSIGG
SVTDAVFSMLNVGSQVAVCWQWATQVQRDYHGPRLLPYIMFPRATIRGIFSLEWFTEQNWSALHEELGGLVRRQELVAHE
TVQDGFEHIPAAYQTLFSASESNRGKVLVRV
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JI7 A 4 ? 354 ? C3PTT2 1 ? 351 ? 1 351 
2 1 9JI7 B 4 ? 354 ? C3PTT2 1 ? 351 ? 1 351 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JI7 LEU A 1 ? UNP C3PTT2 ? ? 'expression tag' -2 1 
1 9JI7 GLY A 2 ? UNP C3PTT2 ? ? 'expression tag' -1 2 
1 9JI7 SER A 3 ? UNP C3PTT2 ? ? 'expression tag' 0  3 
2 9JI7 LEU B 1 ? UNP C3PTT2 ? ? 'expression tag' -2 4 
2 9JI7 GLY B 2 ? UNP C3PTT2 ? ? 'expression tag' -1 5 
2 9JI7 SER B 3 ? UNP C3PTT2 ? ? 'expression tag' 0  6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6070  ? 
1 MORE         -33   ? 
1 'SSA (A^2)'  27280 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 20  ? ILE A 24  ? ASP A 17  ILE A 21  1 ? 5  
HELX_P HELX_P2  AA2 TYR A 53  ? ASP A 60  ? TYR A 50  ASP A 57  1 ? 8  
HELX_P HELX_P3  AA3 ASP A 125 ? TYR A 129 ? ASP A 122 TYR A 126 5 ? 5  
HELX_P HELX_P4  AA4 PRO A 134 ? GLY A 140 ? PRO A 131 GLY A 137 5 ? 7  
HELX_P HELX_P5  AA5 GLY A 143 ? PHE A 156 ? GLY A 140 PHE A 153 1 ? 14 
HELX_P HELX_P6  AA6 GLY A 172 ? ALA A 185 ? GLY A 169 ALA A 182 1 ? 14 
HELX_P HELX_P7  AA7 SER A 195 ? LEU A 205 ? SER A 192 LEU A 202 1 ? 11 
HELX_P HELX_P8  AA8 ASP A 218 ? ALA A 230 ? ASP A 215 ALA A 227 1 ? 13 
HELX_P HELX_P9  AA9 GLY A 242 ? SER A 251 ? GLY A 239 SER A 248 1 ? 10 
HELX_P HELX_P10 AB1 GLN A 264 ? VAL A 269 ? GLN A 261 VAL A 266 1 ? 6  
HELX_P HELX_P11 AB2 LEU A 278 ? ILE A 282 ? LEU A 275 ILE A 279 5 ? 5  
HELX_P HELX_P12 AB3 PHE A 293 ? PHE A 298 ? PHE A 290 PHE A 295 5 ? 6  
HELX_P HELX_P13 AB4 THR A 299 ? ARG A 316 ? THR A 296 ARG A 313 1 ? 18 
HELX_P HELX_P14 AB5 HIS A 331 ? THR A 338 ? HIS A 328 THR A 335 1 ? 8  
HELX_P HELX_P15 AB6 LEU A 339 ? SER A 341 ? LEU A 336 SER A 338 5 ? 3  
HELX_P HELX_P16 AB7 ASP B 20  ? ILE B 24  ? ASP B 17  ILE B 21  1 ? 5  
HELX_P HELX_P17 AB8 TYR B 53  ? ASP B 60  ? TYR B 50  ASP B 57  1 ? 8  
HELX_P HELX_P18 AB9 ASP B 125 ? TYR B 129 ? ASP B 122 TYR B 126 5 ? 5  
HELX_P HELX_P19 AC1 PRO B 134 ? GLY B 140 ? PRO B 131 GLY B 137 5 ? 7  
HELX_P HELX_P20 AC2 GLY B 143 ? PHE B 156 ? GLY B 140 PHE B 153 1 ? 14 
HELX_P HELX_P21 AC3 GLY B 172 ? ALA B 185 ? GLY B 169 ALA B 182 1 ? 14 
HELX_P HELX_P22 AC4 SER B 195 ? GLN B 204 ? SER B 192 GLN B 201 1 ? 10 
HELX_P HELX_P23 AC5 ASP B 218 ? ALA B 230 ? ASP B 215 ALA B 227 1 ? 13 
HELX_P HELX_P24 AC6 GLY B 242 ? SER B 251 ? GLY B 239 SER B 248 1 ? 10 
HELX_P HELX_P25 AC7 GLN B 264 ? VAL B 269 ? GLN B 261 VAL B 266 1 ? 6  
HELX_P HELX_P26 AC8 LEU B 278 ? ILE B 282 ? LEU B 275 ILE B 279 5 ? 5  
HELX_P HELX_P27 AC9 PHE B 293 ? PHE B 298 ? PHE B 290 PHE B 295 5 ? 6  
HELX_P HELX_P28 AD1 THR B 299 ? ARG B 316 ? THR B 296 ARG B 313 1 ? 18 
HELX_P HELX_P29 AD2 HIS B 331 ? ALA B 342 ? HIS B 328 ALA B 339 1 ? 12 
HELX_P HELX_P30 AD3 SER B 343 ? ASN B 346 ? SER B 340 ASN B 343 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 5  ? 
AA3 ? 4  ? 
AA4 ? 2  ? 
AA5 ? 12 ? 
AA6 ? 2  ? 
AA7 ? 2  ? 
AA8 ? 5  ? 
AA9 ? 4  ? 
AB1 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA3 1  2  ? anti-parallel 
AA3 2  3  ? anti-parallel 
AA3 3  4  ? parallel      
AA4 1  2  ? anti-parallel 
AA5 1  2  ? parallel      
AA5 2  3  ? parallel      
AA5 3  4  ? parallel      
AA5 4  5  ? parallel      
AA5 5  6  ? parallel      
AA5 6  7  ? anti-parallel 
AA5 7  8  ? parallel      
AA5 8  9  ? parallel      
AA5 9  10 ? parallel      
AA5 10 11 ? parallel      
AA5 11 12 ? parallel      
AA6 1  2  ? anti-parallel 
AA7 1  2  ? anti-parallel 
AA8 1  2  ? anti-parallel 
AA8 2  3  ? anti-parallel 
AA8 3  4  ? anti-parallel 
AA8 4  5  ? anti-parallel 
AA9 1  2  ? anti-parallel 
AA9 2  3  ? anti-parallel 
AA9 3  4  ? parallel      
AB1 1  2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  SER A 3   ? VAL A 11  ? SER A 0   VAL A 8   
AA1 2  TYR A 25  ? ASN A 33  ? TYR A 22  ASN A 30  
AA2 1  HIS A 99  ? SER A 102 ? HIS A 96  SER A 99  
AA2 2  MET A 41  ? SER A 49  ? MET A 38  SER A 46  
AA2 3  SER A 71  ? ALA A 78  ? SER A 68  ALA A 75  
AA2 4  LEU A 89  ? GLY A 92  ? LEU A 86  GLY A 89  
AA2 5  ARG A 122 ? LEU A 124 ? ARG A 119 LEU A 121 
AA3 1  HIS A 99  ? SER A 102 ? HIS A 96  SER A 99  
AA3 2  MET A 41  ? SER A 49  ? MET A 38  SER A 46  
AA3 3  LYS A 349 ? ARG A 353 ? LYS A 346 ARG A 350 
AA3 4  GLU A 323 ? ASP A 327 ? GLU A 320 ASP A 324 
AA4 1  LYS A 107 ? LEU A 108 ? LYS A 104 LEU A 105 
AA4 2  VAL A 117 ? PHE A 118 ? VAL A 114 PHE A 115 
AA5 1  ALA A 209 ? ASP A 212 ? ALA A 206 ASP A 209 
AA5 2  ARG A 188 ? ALA A 193 ? ARG A 185 ALA A 190 
AA5 3  THR A 164 ? VAL A 167 ? THR A 161 VAL A 164 
AA5 4  VAL A 234 ? ASP A 239 ? VAL A 231 ASP A 236 
AA5 5  LEU A 253 ? VAL A 261 ? LEU A 250 VAL A 258 
AA5 6  THR A 288 ? GLY A 291 ? THR A 285 GLY A 288 
AA5 7  THR B 288 ? GLY B 291 ? THR B 285 GLY B 288 
AA5 8  LEU B 253 ? VAL B 261 ? LEU B 250 VAL B 258 
AA5 9  VAL B 234 ? ASP B 239 ? VAL B 231 ASP B 236 
AA5 10 THR B 164 ? VAL B 167 ? THR B 161 VAL B 164 
AA5 11 ARG B 188 ? ALA B 193 ? ARG B 185 ALA B 190 
AA5 12 ALA B 209 ? ASP B 212 ? ALA B 206 ASP B 209 
AA6 1  HIS A 274 ? PRO A 276 ? HIS A 271 PRO A 273 
AA6 2  HIS B 274 ? PRO B 276 ? HIS B 271 PRO B 273 
AA7 1  SER B 3   ? VAL B 11  ? SER B 0   VAL B 8   
AA7 2  TYR B 25  ? ASN B 33  ? TYR B 22  ASN B 30  
AA8 1  HIS B 99  ? SER B 102 ? HIS B 96  SER B 99  
AA8 2  MET B 41  ? SER B 49  ? MET B 38  SER B 46  
AA8 3  SER B 71  ? ALA B 78  ? SER B 68  ALA B 75  
AA8 4  LEU B 89  ? GLY B 92  ? LEU B 86  GLY B 89  
AA8 5  ARG B 122 ? LEU B 124 ? ARG B 119 LEU B 121 
AA9 1  HIS B 99  ? SER B 102 ? HIS B 96  SER B 99  
AA9 2  MET B 41  ? SER B 49  ? MET B 38  SER B 46  
AA9 3  LYS B 349 ? ARG B 353 ? LYS B 346 ARG B 350 
AA9 4  GLU B 323 ? ASP B 327 ? GLU B 320 ASP B 324 
AB1 1  LYS B 107 ? LEU B 108 ? LYS B 104 LEU B 105 
AB1 2  VAL B 117 ? PHE B 118 ? VAL B 114 PHE B 115 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N THR A 6   ? N THR A 3   O THR A 30  ? O THR A 27  
AA2 1  2  O LEU A 100 ? O LEU A 97  N LEU A 43  ? N LEU A 40  
AA2 2  3  N LEU A 42  ? N LEU A 39  O LEU A 76  ? O LEU A 73  
AA2 3  4  N MET A 73  ? N MET A 70  O VAL A 90  ? O VAL A 87  
AA2 4  5  N GLN A 91  ? N GLN A 88  O ARG A 122 ? O ARG A 119 
AA3 1  2  O LEU A 100 ? O LEU A 97  N LEU A 43  ? N LEU A 40  
AA3 2  3  N VAL A 48  ? N VAL A 45  O VAL A 352 ? O VAL A 349 
AA3 3  4  O ARG A 353 ? O ARG A 350 N GLN A 326 ? N GLN A 323 
AA4 1  2  N LYS A 107 ? N LYS A 104 O PHE A 118 ? O PHE A 115 
AA5 1  2  O ILE A 211 ? O ILE A 208 N GLY A 191 ? N GLY A 188 
AA5 2  3  O ARG A 188 ? O ARG A 185 N VAL A 165 ? N VAL A 162 
AA5 3  4  N VAL A 166 ? N VAL A 163 O PHE A 238 ? O PHE A 235 
AA5 4  5  N TYR A 237 ? N TYR A 234 O ALA A 260 ? O ALA A 257 
AA5 5  6  N VAL A 259 ? N VAL A 256 O THR A 288 ? O THR A 285 
AA5 6  7  N ILE A 289 ? N ILE A 286 O ILE B 289 ? O ILE B 286 
AA5 7  8  O THR B 288 ? O THR B 285 N VAL B 259 ? N VAL B 256 
AA5 8  9  O ALA B 260 ? O ALA B 257 N TYR B 237 ? N TYR B 234 
AA5 9  10 O LYS B 236 ? O LYS B 233 N VAL B 166 ? N VAL B 163 
AA5 10 11 N VAL B 165 ? N VAL B 162 O ARG B 188 ? O ARG B 185 
AA5 11 12 N GLY B 191 ? N GLY B 188 O ILE B 211 ? O ILE B 208 
AA6 1  2  N GLY A 275 ? N GLY A 272 O GLY B 275 ? O GLY B 272 
AA7 1  2  N THR B 6   ? N THR B 3   O THR B 30  ? O THR B 27  
AA8 1  2  O SER B 102 ? O SER B 99  N MET B 41  ? N MET B 38  
AA8 2  3  N LEU B 46  ? N LEU B 43  O ILE B 72  ? O ILE B 69  
AA8 3  4  N SER B 71  ? N SER B 68  O GLY B 92  ? O GLY B 89  
AA8 4  5  N LEU B 89  ? N LEU B 86  O LEU B 124 ? O LEU B 121 
AA9 1  2  O SER B 102 ? O SER B 99  N MET B 41  ? N MET B 38  
AA9 2  3  N VAL B 48  ? N VAL B 45  O VAL B 352 ? O VAL B 349 
AA9 3  4  O ARG B 353 ? O ARG B 350 N GLN B 326 ? N GLN B 323 
AB1 1  2  N LYS B 107 ? N LYS B 104 O PHE B 118 ? O PHE B 115 
# 
_pdbx_entry_details.entry_id                   9JI7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A 153 ? ? -138.60 -65.68  
2 1 ASN B 78  ? ? -91.97  38.45   
3 1 ASP B 127 ? ? -161.13 -163.82 
4 1 LEU B 130 ? ? -114.90 77.79   
5 1 PHE B 153 ? ? -128.26 -68.30  
6 1 PHE B 290 ? ? -153.19 80.43   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1EBZ C8   C N S 1   
A1EBZ C5   C N N 2   
A1EBZ C6   C N S 3   
A1EBZ N1   N N N 4   
A1EBZ C2   C N N 5   
A1EBZ C4   C N S 6   
A1EBZ C21  C N N 7   
A1EBZ C23  C N N 8   
A1EBZ C24  C N N 9   
A1EBZ C25  C N N 10  
A1EBZ C27  C N N 11  
A1EBZ C29  C N N 12  
A1EBZ C1   C N N 13  
A1EBZ C10  C N N 14  
A1EBZ C11  C N N 15  
A1EBZ C12  C N N 16  
A1EBZ C13  C N N 17  
A1EBZ C14  C N N 18  
A1EBZ C15  C N N 19  
A1EBZ C16  C N N 20  
A1EBZ C17  C N S 21  
A1EBZ C18  C N N 22  
A1EBZ C19  C N N 23  
A1EBZ C20  C N N 24  
A1EBZ C22  C N N 25  
A1EBZ C26  C N S 26  
A1EBZ C28  C N R 27  
A1EBZ C3   C N R 28  
A1EBZ C7   C N R 29  
A1EBZ C9   C N N 30  
A1EBZ N2   N N N 31  
A1EBZ O1   O N N 32  
A1EBZ O2   O N N 33  
A1EBZ O3   O N N 34  
A1EBZ O4   O N N 35  
A1EBZ O5   O N N 36  
A1EBZ H1   H N N 37  
A1EBZ H2   H N N 38  
A1EBZ H3   H N N 39  
A1EBZ H4   H N N 40  
A1EBZ H5   H N N 41  
A1EBZ H6   H N N 42  
A1EBZ H7   H N N 43  
A1EBZ H8   H N N 44  
A1EBZ H9   H N N 45  
A1EBZ H10  H N N 46  
A1EBZ H12  H N N 47  
A1EBZ H13  H N N 48  
A1EBZ H14  H N N 49  
A1EBZ H15  H N N 50  
A1EBZ H16  H N N 51  
A1EBZ H17  H N N 52  
A1EBZ H18  H N N 53  
A1EBZ H19  H N N 54  
A1EBZ H20  H N N 55  
A1EBZ H21  H N N 56  
A1EBZ H22  H N N 57  
A1EBZ H23  H N N 58  
A1EBZ H24  H N N 59  
A1EBZ H25  H N N 60  
A1EBZ H26  H N N 61  
A1EBZ H27  H N N 62  
A1EBZ H28  H N N 63  
A1EBZ H29  H N N 64  
A1EBZ H30  H N N 65  
A1EBZ H32  H N N 66  
A1EBZ H33  H N N 67  
A1EBZ H34  H N N 68  
A1EBZ H35  H N N 69  
A1EBZ H36  H N N 70  
A1EBZ H37  H N N 71  
A1EBZ H38  H N N 72  
A1EBZ H39  H N N 73  
A1EBZ H40  H N N 74  
ALA   N    N N N 75  
ALA   CA   C N S 76  
ALA   C    C N N 77  
ALA   O    O N N 78  
ALA   CB   C N N 79  
ALA   OXT  O N N 80  
ALA   H    H N N 81  
ALA   H2   H N N 82  
ALA   HA   H N N 83  
ALA   HB1  H N N 84  
ALA   HB2  H N N 85  
ALA   HB3  H N N 86  
ALA   HXT  H N N 87  
ARG   N    N N N 88  
ARG   CA   C N S 89  
ARG   C    C N N 90  
ARG   O    O N N 91  
ARG   CB   C N N 92  
ARG   CG   C N N 93  
ARG   CD   C N N 94  
ARG   NE   N N N 95  
ARG   CZ   C N N 96  
ARG   NH1  N N N 97  
ARG   NH2  N N N 98  
ARG   OXT  O N N 99  
ARG   H    H N N 100 
ARG   H2   H N N 101 
ARG   HA   H N N 102 
ARG   HB2  H N N 103 
ARG   HB3  H N N 104 
ARG   HG2  H N N 105 
ARG   HG3  H N N 106 
ARG   HD2  H N N 107 
ARG   HD3  H N N 108 
ARG   HE   H N N 109 
ARG   HH11 H N N 110 
ARG   HH12 H N N 111 
ARG   HH21 H N N 112 
ARG   HH22 H N N 113 
ARG   HXT  H N N 114 
ASN   N    N N N 115 
ASN   CA   C N S 116 
ASN   C    C N N 117 
ASN   O    O N N 118 
ASN   CB   C N N 119 
ASN   CG   C N N 120 
ASN   OD1  O N N 121 
ASN   ND2  N N N 122 
ASN   OXT  O N N 123 
ASN   H    H N N 124 
ASN   H2   H N N 125 
ASN   HA   H N N 126 
ASN   HB2  H N N 127 
ASN   HB3  H N N 128 
ASN   HD21 H N N 129 
ASN   HD22 H N N 130 
ASN   HXT  H N N 131 
ASP   N    N N N 132 
ASP   CA   C N S 133 
ASP   C    C N N 134 
ASP   O    O N N 135 
ASP   CB   C N N 136 
ASP   CG   C N N 137 
ASP   OD1  O N N 138 
ASP   OD2  O N N 139 
ASP   OXT  O N N 140 
ASP   H    H N N 141 
ASP   H2   H N N 142 
ASP   HA   H N N 143 
ASP   HB2  H N N 144 
ASP   HB3  H N N 145 
ASP   HD2  H N N 146 
ASP   HXT  H N N 147 
CYS   N    N N N 148 
CYS   CA   C N R 149 
CYS   C    C N N 150 
CYS   O    O N N 151 
CYS   CB   C N N 152 
CYS   SG   S N N 153 
CYS   OXT  O N N 154 
CYS   H    H N N 155 
CYS   H2   H N N 156 
CYS   HA   H N N 157 
CYS   HB2  H N N 158 
CYS   HB3  H N N 159 
CYS   HG   H N N 160 
CYS   HXT  H N N 161 
GLN   N    N N N 162 
GLN   CA   C N S 163 
GLN   C    C N N 164 
GLN   O    O N N 165 
GLN   CB   C N N 166 
GLN   CG   C N N 167 
GLN   CD   C N N 168 
GLN   OE1  O N N 169 
GLN   NE2  N N N 170 
GLN   OXT  O N N 171 
GLN   H    H N N 172 
GLN   H2   H N N 173 
GLN   HA   H N N 174 
GLN   HB2  H N N 175 
GLN   HB3  H N N 176 
GLN   HG2  H N N 177 
GLN   HG3  H N N 178 
GLN   HE21 H N N 179 
GLN   HE22 H N N 180 
GLN   HXT  H N N 181 
GLU   N    N N N 182 
GLU   CA   C N S 183 
GLU   C    C N N 184 
GLU   O    O N N 185 
GLU   CB   C N N 186 
GLU   CG   C N N 187 
GLU   CD   C N N 188 
GLU   OE1  O N N 189 
GLU   OE2  O N N 190 
GLU   OXT  O N N 191 
GLU   H    H N N 192 
GLU   H2   H N N 193 
GLU   HA   H N N 194 
GLU   HB2  H N N 195 
GLU   HB3  H N N 196 
GLU   HG2  H N N 197 
GLU   HG3  H N N 198 
GLU   HE2  H N N 199 
GLU   HXT  H N N 200 
GLY   N    N N N 201 
GLY   CA   C N N 202 
GLY   C    C N N 203 
GLY   O    O N N 204 
GLY   OXT  O N N 205 
GLY   H    H N N 206 
GLY   H2   H N N 207 
GLY   HA2  H N N 208 
GLY   HA3  H N N 209 
GLY   HXT  H N N 210 
HIS   N    N N N 211 
HIS   CA   C N S 212 
HIS   C    C N N 213 
HIS   O    O N N 214 
HIS   CB   C N N 215 
HIS   CG   C Y N 216 
HIS   ND1  N Y N 217 
HIS   CD2  C Y N 218 
HIS   CE1  C Y N 219 
HIS   NE2  N Y N 220 
HIS   OXT  O N N 221 
HIS   H    H N N 222 
HIS   H2   H N N 223 
HIS   HA   H N N 224 
HIS   HB2  H N N 225 
HIS   HB3  H N N 226 
HIS   HD1  H N N 227 
HIS   HD2  H N N 228 
HIS   HE1  H N N 229 
HIS   HE2  H N N 230 
HIS   HXT  H N N 231 
HOH   O    O N N 232 
HOH   H1   H N N 233 
HOH   H2   H N N 234 
ILE   N    N N N 235 
ILE   CA   C N S 236 
ILE   C    C N N 237 
ILE   O    O N N 238 
ILE   CB   C N S 239 
ILE   CG1  C N N 240 
ILE   CG2  C N N 241 
ILE   CD1  C N N 242 
ILE   OXT  O N N 243 
ILE   H    H N N 244 
ILE   H2   H N N 245 
ILE   HA   H N N 246 
ILE   HB   H N N 247 
ILE   HG12 H N N 248 
ILE   HG13 H N N 249 
ILE   HG21 H N N 250 
ILE   HG22 H N N 251 
ILE   HG23 H N N 252 
ILE   HD11 H N N 253 
ILE   HD12 H N N 254 
ILE   HD13 H N N 255 
ILE   HXT  H N N 256 
LEU   N    N N N 257 
LEU   CA   C N S 258 
LEU   C    C N N 259 
LEU   O    O N N 260 
LEU   CB   C N N 261 
LEU   CG   C N N 262 
LEU   CD1  C N N 263 
LEU   CD2  C N N 264 
LEU   OXT  O N N 265 
LEU   H    H N N 266 
LEU   H2   H N N 267 
LEU   HA   H N N 268 
LEU   HB2  H N N 269 
LEU   HB3  H N N 270 
LEU   HG   H N N 271 
LEU   HD11 H N N 272 
LEU   HD12 H N N 273 
LEU   HD13 H N N 274 
LEU   HD21 H N N 275 
LEU   HD22 H N N 276 
LEU   HD23 H N N 277 
LEU   HXT  H N N 278 
LYS   N    N N N 279 
LYS   CA   C N S 280 
LYS   C    C N N 281 
LYS   O    O N N 282 
LYS   CB   C N N 283 
LYS   CG   C N N 284 
LYS   CD   C N N 285 
LYS   CE   C N N 286 
LYS   NZ   N N N 287 
LYS   OXT  O N N 288 
LYS   H    H N N 289 
LYS   H2   H N N 290 
LYS   HA   H N N 291 
LYS   HB2  H N N 292 
LYS   HB3  H N N 293 
LYS   HG2  H N N 294 
LYS   HG3  H N N 295 
LYS   HD2  H N N 296 
LYS   HD3  H N N 297 
LYS   HE2  H N N 298 
LYS   HE3  H N N 299 
LYS   HZ1  H N N 300 
LYS   HZ2  H N N 301 
LYS   HZ3  H N N 302 
LYS   HXT  H N N 303 
MET   N    N N N 304 
MET   CA   C N S 305 
MET   C    C N N 306 
MET   O    O N N 307 
MET   CB   C N N 308 
MET   CG   C N N 309 
MET   SD   S N N 310 
MET   CE   C N N 311 
MET   OXT  O N N 312 
MET   H    H N N 313 
MET   H2   H N N 314 
MET   HA   H N N 315 
MET   HB2  H N N 316 
MET   HB3  H N N 317 
MET   HG2  H N N 318 
MET   HG3  H N N 319 
MET   HE1  H N N 320 
MET   HE2  H N N 321 
MET   HE3  H N N 322 
MET   HXT  H N N 323 
NAP   PA   P N R 324 
NAP   O1A  O N N 325 
NAP   O2A  O N N 326 
NAP   O5B  O N N 327 
NAP   C5B  C N N 328 
NAP   C4B  C N R 329 
NAP   O4B  O N N 330 
NAP   C3B  C N R 331 
NAP   O3B  O N N 332 
NAP   C2B  C N R 333 
NAP   O2B  O N N 334 
NAP   C1B  C N R 335 
NAP   N9A  N Y N 336 
NAP   C8A  C Y N 337 
NAP   N7A  N Y N 338 
NAP   C5A  C Y N 339 
NAP   C6A  C Y N 340 
NAP   N6A  N N N 341 
NAP   N1A  N Y N 342 
NAP   C2A  C Y N 343 
NAP   N3A  N Y N 344 
NAP   C4A  C Y N 345 
NAP   O3   O N N 346 
NAP   PN   P N N 347 
NAP   O1N  O N N 348 
NAP   O2N  O N N 349 
NAP   O5D  O N N 350 
NAP   C5D  C N N 351 
NAP   C4D  C N R 352 
NAP   O4D  O N N 353 
NAP   C3D  C N S 354 
NAP   O3D  O N N 355 
NAP   C2D  C N R 356 
NAP   O2D  O N N 357 
NAP   C1D  C N R 358 
NAP   N1N  N Y N 359 
NAP   C2N  C Y N 360 
NAP   C3N  C Y N 361 
NAP   C7N  C N N 362 
NAP   O7N  O N N 363 
NAP   N7N  N N N 364 
NAP   C4N  C Y N 365 
NAP   C5N  C Y N 366 
NAP   C6N  C Y N 367 
NAP   P2B  P N N 368 
NAP   O1X  O N N 369 
NAP   O2X  O N N 370 
NAP   O3X  O N N 371 
NAP   HOA2 H N N 372 
NAP   H51A H N N 373 
NAP   H52A H N N 374 
NAP   H4B  H N N 375 
NAP   H3B  H N N 376 
NAP   HO3A H N N 377 
NAP   H2B  H N N 378 
NAP   H1B  H N N 379 
NAP   H8A  H N N 380 
NAP   H61A H N N 381 
NAP   H62A H N N 382 
NAP   H2A  H N N 383 
NAP   H51N H N N 384 
NAP   H52N H N N 385 
NAP   H4D  H N N 386 
NAP   H3D  H N N 387 
NAP   HO3N H N N 388 
NAP   H2D  H N N 389 
NAP   HO2N H N N 390 
NAP   H1D  H N N 391 
NAP   H2N  H N N 392 
NAP   H71N H N N 393 
NAP   H72N H N N 394 
NAP   H4N  H N N 395 
NAP   H5N  H N N 396 
NAP   H6N  H N N 397 
NAP   HOP2 H N N 398 
NAP   HOP3 H N N 399 
PHE   N    N N N 400 
PHE   CA   C N S 401 
PHE   C    C N N 402 
PHE   O    O N N 403 
PHE   CB   C N N 404 
PHE   CG   C Y N 405 
PHE   CD1  C Y N 406 
PHE   CD2  C Y N 407 
PHE   CE1  C Y N 408 
PHE   CE2  C Y N 409 
PHE   CZ   C Y N 410 
PHE   OXT  O N N 411 
PHE   H    H N N 412 
PHE   H2   H N N 413 
PHE   HA   H N N 414 
PHE   HB2  H N N 415 
PHE   HB3  H N N 416 
PHE   HD1  H N N 417 
PHE   HD2  H N N 418 
PHE   HE1  H N N 419 
PHE   HE2  H N N 420 
PHE   HZ   H N N 421 
PHE   HXT  H N N 422 
PRO   N    N N N 423 
PRO   CA   C N S 424 
PRO   C    C N N 425 
PRO   O    O N N 426 
PRO   CB   C N N 427 
PRO   CG   C N N 428 
PRO   CD   C N N 429 
PRO   OXT  O N N 430 
PRO   H    H N N 431 
PRO   HA   H N N 432 
PRO   HB2  H N N 433 
PRO   HB3  H N N 434 
PRO   HG2  H N N 435 
PRO   HG3  H N N 436 
PRO   HD2  H N N 437 
PRO   HD3  H N N 438 
PRO   HXT  H N N 439 
SER   N    N N N 440 
SER   CA   C N S 441 
SER   C    C N N 442 
SER   O    O N N 443 
SER   CB   C N N 444 
SER   OG   O N N 445 
SER   OXT  O N N 446 
SER   H    H N N 447 
SER   H2   H N N 448 
SER   HA   H N N 449 
SER   HB2  H N N 450 
SER   HB3  H N N 451 
SER   HG   H N N 452 
SER   HXT  H N N 453 
THR   N    N N N 454 
THR   CA   C N S 455 
THR   C    C N N 456 
THR   O    O N N 457 
THR   CB   C N R 458 
THR   OG1  O N N 459 
THR   CG2  C N N 460 
THR   OXT  O N N 461 
THR   H    H N N 462 
THR   H2   H N N 463 
THR   HA   H N N 464 
THR   HB   H N N 465 
THR   HG1  H N N 466 
THR   HG21 H N N 467 
THR   HG22 H N N 468 
THR   HG23 H N N 469 
THR   HXT  H N N 470 
TRP   N    N N N 471 
TRP   CA   C N S 472 
TRP   C    C N N 473 
TRP   O    O N N 474 
TRP   CB   C N N 475 
TRP   CG   C Y N 476 
TRP   CD1  C Y N 477 
TRP   CD2  C Y N 478 
TRP   NE1  N Y N 479 
TRP   CE2  C Y N 480 
TRP   CE3  C Y N 481 
TRP   CZ2  C Y N 482 
TRP   CZ3  C Y N 483 
TRP   CH2  C Y N 484 
TRP   OXT  O N N 485 
TRP   H    H N N 486 
TRP   H2   H N N 487 
TRP   HA   H N N 488 
TRP   HB2  H N N 489 
TRP   HB3  H N N 490 
TRP   HD1  H N N 491 
TRP   HE1  H N N 492 
TRP   HE3  H N N 493 
TRP   HZ2  H N N 494 
TRP   HZ3  H N N 495 
TRP   HH2  H N N 496 
TRP   HXT  H N N 497 
TYR   N    N N N 498 
TYR   CA   C N S 499 
TYR   C    C N N 500 
TYR   O    O N N 501 
TYR   CB   C N N 502 
TYR   CG   C Y N 503 
TYR   CD1  C Y N 504 
TYR   CD2  C Y N 505 
TYR   CE1  C Y N 506 
TYR   CE2  C Y N 507 
TYR   CZ   C Y N 508 
TYR   OH   O N N 509 
TYR   OXT  O N N 510 
TYR   H    H N N 511 
TYR   H2   H N N 512 
TYR   HA   H N N 513 
TYR   HB2  H N N 514 
TYR   HB3  H N N 515 
TYR   HD1  H N N 516 
TYR   HD2  H N N 517 
TYR   HE1  H N N 518 
TYR   HE2  H N N 519 
TYR   HH   H N N 520 
TYR   HXT  H N N 521 
VAL   N    N N N 522 
VAL   CA   C N S 523 
VAL   C    C N N 524 
VAL   O    O N N 525 
VAL   CB   C N N 526 
VAL   CG1  C N N 527 
VAL   CG2  C N N 528 
VAL   OXT  O N N 529 
VAL   H    H N N 530 
VAL   H2   H N N 531 
VAL   HA   H N N 532 
VAL   HB   H N N 533 
VAL   HG11 H N N 534 
VAL   HG12 H N N 535 
VAL   HG13 H N N 536 
VAL   HG21 H N N 537 
VAL   HG22 H N N 538 
VAL   HG23 H N N 539 
VAL   HXT  H N N 540 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1EBZ O1  C20  doub N N 1   
A1EBZ O2  C21  sing N N 2   
A1EBZ C20 N2   sing N N 3   
A1EBZ C20 C19  sing N N 4   
A1EBZ C21 C19  doub N Z 5   
A1EBZ C21 C22  sing N N 6   
A1EBZ N2  C17  sing N N 7   
A1EBZ C19 C18  sing N N 8   
A1EBZ C23 C22  doub N E 9   
A1EBZ C23 C24  sing N N 10  
A1EBZ C17 C18  sing N N 11  
A1EBZ C17 C16  sing N N 12  
A1EBZ C18 O4   doub N N 13  
A1EBZ C25 C24  doub N E 14  
A1EBZ C25 C26  sing N N 15  
A1EBZ O3  C26  sing N N 16  
A1EBZ C26 C7   sing N N 17  
A1EBZ C16 C15  sing N N 18  
A1EBZ O5  C13  doub N N 19  
A1EBZ N1  C13  sing N N 20  
A1EBZ N1  C14  sing N N 21  
A1EBZ C13 C12  sing N N 22  
A1EBZ C15 C14  sing N N 23  
A1EBZ C7  C8   sing N N 24  
A1EBZ C7  C6   sing N N 25  
A1EBZ C5  C4   sing N N 26  
A1EBZ C12 C11  doub N E 27  
A1EBZ C11 C10  sing N N 28  
A1EBZ C8  C9   sing N N 29  
A1EBZ C8  C27  sing N N 30  
A1EBZ C4  C6   sing N N 31  
A1EBZ C4  C3   sing N N 32  
A1EBZ C6  C28  sing N N 33  
A1EBZ C10 C9   doub N Z 34  
A1EBZ C27 C28  sing N N 35  
A1EBZ C28 C29  sing N N 36  
A1EBZ C3  C2   sing N N 37  
A1EBZ C3  C29  sing N N 38  
A1EBZ C2  C1   sing N N 39  
A1EBZ C8  H1   sing N N 40  
A1EBZ C5  H2   sing N N 41  
A1EBZ C5  H3   sing N N 42  
A1EBZ C5  H4   sing N N 43  
A1EBZ C6  H5   sing N N 44  
A1EBZ N1  H6   sing N N 45  
A1EBZ C2  H7   sing N N 46  
A1EBZ C2  H8   sing N N 47  
A1EBZ C4  H9   sing N N 48  
A1EBZ C23 H10  sing N N 49  
A1EBZ C24 H12  sing N N 50  
A1EBZ C25 H13  sing N N 51  
A1EBZ C27 H14  sing N N 52  
A1EBZ C27 H15  sing N N 53  
A1EBZ C29 H16  sing N N 54  
A1EBZ C29 H17  sing N N 55  
A1EBZ C1  H18  sing N N 56  
A1EBZ C1  H19  sing N N 57  
A1EBZ C1  H20  sing N N 58  
A1EBZ C10 H21  sing N N 59  
A1EBZ C11 H22  sing N N 60  
A1EBZ C12 H23  sing N N 61  
A1EBZ C14 H24  sing N N 62  
A1EBZ C14 H25  sing N N 63  
A1EBZ C15 H26  sing N N 64  
A1EBZ C15 H27  sing N N 65  
A1EBZ C16 H28  sing N N 66  
A1EBZ C16 H29  sing N N 67  
A1EBZ C17 H30  sing N N 68  
A1EBZ C22 H32  sing N N 69  
A1EBZ C26 H33  sing N N 70  
A1EBZ C28 H34  sing N N 71  
A1EBZ C3  H35  sing N N 72  
A1EBZ C7  H36  sing N N 73  
A1EBZ C9  H37  sing N N 74  
A1EBZ N2  H38  sing N N 75  
A1EBZ O2  H39  sing N N 76  
A1EBZ O3  H40  sing N N 77  
ALA   N   CA   sing N N 78  
ALA   N   H    sing N N 79  
ALA   N   H2   sing N N 80  
ALA   CA  C    sing N N 81  
ALA   CA  CB   sing N N 82  
ALA   CA  HA   sing N N 83  
ALA   C   O    doub N N 84  
ALA   C   OXT  sing N N 85  
ALA   CB  HB1  sing N N 86  
ALA   CB  HB2  sing N N 87  
ALA   CB  HB3  sing N N 88  
ALA   OXT HXT  sing N N 89  
ARG   N   CA   sing N N 90  
ARG   N   H    sing N N 91  
ARG   N   H2   sing N N 92  
ARG   CA  C    sing N N 93  
ARG   CA  CB   sing N N 94  
ARG   CA  HA   sing N N 95  
ARG   C   O    doub N N 96  
ARG   C   OXT  sing N N 97  
ARG   CB  CG   sing N N 98  
ARG   CB  HB2  sing N N 99  
ARG   CB  HB3  sing N N 100 
ARG   CG  CD   sing N N 101 
ARG   CG  HG2  sing N N 102 
ARG   CG  HG3  sing N N 103 
ARG   CD  NE   sing N N 104 
ARG   CD  HD2  sing N N 105 
ARG   CD  HD3  sing N N 106 
ARG   NE  CZ   sing N N 107 
ARG   NE  HE   sing N N 108 
ARG   CZ  NH1  sing N N 109 
ARG   CZ  NH2  doub N N 110 
ARG   NH1 HH11 sing N N 111 
ARG   NH1 HH12 sing N N 112 
ARG   NH2 HH21 sing N N 113 
ARG   NH2 HH22 sing N N 114 
ARG   OXT HXT  sing N N 115 
ASN   N   CA   sing N N 116 
ASN   N   H    sing N N 117 
ASN   N   H2   sing N N 118 
ASN   CA  C    sing N N 119 
ASN   CA  CB   sing N N 120 
ASN   CA  HA   sing N N 121 
ASN   C   O    doub N N 122 
ASN   C   OXT  sing N N 123 
ASN   CB  CG   sing N N 124 
ASN   CB  HB2  sing N N 125 
ASN   CB  HB3  sing N N 126 
ASN   CG  OD1  doub N N 127 
ASN   CG  ND2  sing N N 128 
ASN   ND2 HD21 sing N N 129 
ASN   ND2 HD22 sing N N 130 
ASN   OXT HXT  sing N N 131 
ASP   N   CA   sing N N 132 
ASP   N   H    sing N N 133 
ASP   N   H2   sing N N 134 
ASP   CA  C    sing N N 135 
ASP   CA  CB   sing N N 136 
ASP   CA  HA   sing N N 137 
ASP   C   O    doub N N 138 
ASP   C   OXT  sing N N 139 
ASP   CB  CG   sing N N 140 
ASP   CB  HB2  sing N N 141 
ASP   CB  HB3  sing N N 142 
ASP   CG  OD1  doub N N 143 
ASP   CG  OD2  sing N N 144 
ASP   OD2 HD2  sing N N 145 
ASP   OXT HXT  sing N N 146 
CYS   N   CA   sing N N 147 
CYS   N   H    sing N N 148 
CYS   N   H2   sing N N 149 
CYS   CA  C    sing N N 150 
CYS   CA  CB   sing N N 151 
CYS   CA  HA   sing N N 152 
CYS   C   O    doub N N 153 
CYS   C   OXT  sing N N 154 
CYS   CB  SG   sing N N 155 
CYS   CB  HB2  sing N N 156 
CYS   CB  HB3  sing N N 157 
CYS   SG  HG   sing N N 158 
CYS   OXT HXT  sing N N 159 
GLN   N   CA   sing N N 160 
GLN   N   H    sing N N 161 
GLN   N   H2   sing N N 162 
GLN   CA  C    sing N N 163 
GLN   CA  CB   sing N N 164 
GLN   CA  HA   sing N N 165 
GLN   C   O    doub N N 166 
GLN   C   OXT  sing N N 167 
GLN   CB  CG   sing N N 168 
GLN   CB  HB2  sing N N 169 
GLN   CB  HB3  sing N N 170 
GLN   CG  CD   sing N N 171 
GLN   CG  HG2  sing N N 172 
GLN   CG  HG3  sing N N 173 
GLN   CD  OE1  doub N N 174 
GLN   CD  NE2  sing N N 175 
GLN   NE2 HE21 sing N N 176 
GLN   NE2 HE22 sing N N 177 
GLN   OXT HXT  sing N N 178 
GLU   N   CA   sing N N 179 
GLU   N   H    sing N N 180 
GLU   N   H2   sing N N 181 
GLU   CA  C    sing N N 182 
GLU   CA  CB   sing N N 183 
GLU   CA  HA   sing N N 184 
GLU   C   O    doub N N 185 
GLU   C   OXT  sing N N 186 
GLU   CB  CG   sing N N 187 
GLU   CB  HB2  sing N N 188 
GLU   CB  HB3  sing N N 189 
GLU   CG  CD   sing N N 190 
GLU   CG  HG2  sing N N 191 
GLU   CG  HG3  sing N N 192 
GLU   CD  OE1  doub N N 193 
GLU   CD  OE2  sing N N 194 
GLU   OE2 HE2  sing N N 195 
GLU   OXT HXT  sing N N 196 
GLY   N   CA   sing N N 197 
GLY   N   H    sing N N 198 
GLY   N   H2   sing N N 199 
GLY   CA  C    sing N N 200 
GLY   CA  HA2  sing N N 201 
GLY   CA  HA3  sing N N 202 
GLY   C   O    doub N N 203 
GLY   C   OXT  sing N N 204 
GLY   OXT HXT  sing N N 205 
HIS   N   CA   sing N N 206 
HIS   N   H    sing N N 207 
HIS   N   H2   sing N N 208 
HIS   CA  C    sing N N 209 
HIS   CA  CB   sing N N 210 
HIS   CA  HA   sing N N 211 
HIS   C   O    doub N N 212 
HIS   C   OXT  sing N N 213 
HIS   CB  CG   sing N N 214 
HIS   CB  HB2  sing N N 215 
HIS   CB  HB3  sing N N 216 
HIS   CG  ND1  sing Y N 217 
HIS   CG  CD2  doub Y N 218 
HIS   ND1 CE1  doub Y N 219 
HIS   ND1 HD1  sing N N 220 
HIS   CD2 NE2  sing Y N 221 
HIS   CD2 HD2  sing N N 222 
HIS   CE1 NE2  sing Y N 223 
HIS   CE1 HE1  sing N N 224 
HIS   NE2 HE2  sing N N 225 
HIS   OXT HXT  sing N N 226 
HOH   O   H1   sing N N 227 
HOH   O   H2   sing N N 228 
ILE   N   CA   sing N N 229 
ILE   N   H    sing N N 230 
ILE   N   H2   sing N N 231 
ILE   CA  C    sing N N 232 
ILE   CA  CB   sing N N 233 
ILE   CA  HA   sing N N 234 
ILE   C   O    doub N N 235 
ILE   C   OXT  sing N N 236 
ILE   CB  CG1  sing N N 237 
ILE   CB  CG2  sing N N 238 
ILE   CB  HB   sing N N 239 
ILE   CG1 CD1  sing N N 240 
ILE   CG1 HG12 sing N N 241 
ILE   CG1 HG13 sing N N 242 
ILE   CG2 HG21 sing N N 243 
ILE   CG2 HG22 sing N N 244 
ILE   CG2 HG23 sing N N 245 
ILE   CD1 HD11 sing N N 246 
ILE   CD1 HD12 sing N N 247 
ILE   CD1 HD13 sing N N 248 
ILE   OXT HXT  sing N N 249 
LEU   N   CA   sing N N 250 
LEU   N   H    sing N N 251 
LEU   N   H2   sing N N 252 
LEU   CA  C    sing N N 253 
LEU   CA  CB   sing N N 254 
LEU   CA  HA   sing N N 255 
LEU   C   O    doub N N 256 
LEU   C   OXT  sing N N 257 
LEU   CB  CG   sing N N 258 
LEU   CB  HB2  sing N N 259 
LEU   CB  HB3  sing N N 260 
LEU   CG  CD1  sing N N 261 
LEU   CG  CD2  sing N N 262 
LEU   CG  HG   sing N N 263 
LEU   CD1 HD11 sing N N 264 
LEU   CD1 HD12 sing N N 265 
LEU   CD1 HD13 sing N N 266 
LEU   CD2 HD21 sing N N 267 
LEU   CD2 HD22 sing N N 268 
LEU   CD2 HD23 sing N N 269 
LEU   OXT HXT  sing N N 270 
LYS   N   CA   sing N N 271 
LYS   N   H    sing N N 272 
LYS   N   H2   sing N N 273 
LYS   CA  C    sing N N 274 
LYS   CA  CB   sing N N 275 
LYS   CA  HA   sing N N 276 
LYS   C   O    doub N N 277 
LYS   C   OXT  sing N N 278 
LYS   CB  CG   sing N N 279 
LYS   CB  HB2  sing N N 280 
LYS   CB  HB3  sing N N 281 
LYS   CG  CD   sing N N 282 
LYS   CG  HG2  sing N N 283 
LYS   CG  HG3  sing N N 284 
LYS   CD  CE   sing N N 285 
LYS   CD  HD2  sing N N 286 
LYS   CD  HD3  sing N N 287 
LYS   CE  NZ   sing N N 288 
LYS   CE  HE2  sing N N 289 
LYS   CE  HE3  sing N N 290 
LYS   NZ  HZ1  sing N N 291 
LYS   NZ  HZ2  sing N N 292 
LYS   NZ  HZ3  sing N N 293 
LYS   OXT HXT  sing N N 294 
MET   N   CA   sing N N 295 
MET   N   H    sing N N 296 
MET   N   H2   sing N N 297 
MET   CA  C    sing N N 298 
MET   CA  CB   sing N N 299 
MET   CA  HA   sing N N 300 
MET   C   O    doub N N 301 
MET   C   OXT  sing N N 302 
MET   CB  CG   sing N N 303 
MET   CB  HB2  sing N N 304 
MET   CB  HB3  sing N N 305 
MET   CG  SD   sing N N 306 
MET   CG  HG2  sing N N 307 
MET   CG  HG3  sing N N 308 
MET   SD  CE   sing N N 309 
MET   CE  HE1  sing N N 310 
MET   CE  HE2  sing N N 311 
MET   CE  HE3  sing N N 312 
MET   OXT HXT  sing N N 313 
NAP   PA  O1A  doub N N 314 
NAP   PA  O2A  sing N N 315 
NAP   PA  O5B  sing N N 316 
NAP   PA  O3   sing N N 317 
NAP   O2A HOA2 sing N N 318 
NAP   O5B C5B  sing N N 319 
NAP   C5B C4B  sing N N 320 
NAP   C5B H51A sing N N 321 
NAP   C5B H52A sing N N 322 
NAP   C4B O4B  sing N N 323 
NAP   C4B C3B  sing N N 324 
NAP   C4B H4B  sing N N 325 
NAP   O4B C1B  sing N N 326 
NAP   C3B O3B  sing N N 327 
NAP   C3B C2B  sing N N 328 
NAP   C3B H3B  sing N N 329 
NAP   O3B HO3A sing N N 330 
NAP   C2B O2B  sing N N 331 
NAP   C2B C1B  sing N N 332 
NAP   C2B H2B  sing N N 333 
NAP   O2B P2B  sing N N 334 
NAP   C1B N9A  sing N N 335 
NAP   C1B H1B  sing N N 336 
NAP   N9A C8A  sing Y N 337 
NAP   N9A C4A  sing Y N 338 
NAP   C8A N7A  doub Y N 339 
NAP   C8A H8A  sing N N 340 
NAP   N7A C5A  sing Y N 341 
NAP   C5A C6A  sing Y N 342 
NAP   C5A C4A  doub Y N 343 
NAP   C6A N6A  sing N N 344 
NAP   C6A N1A  doub Y N 345 
NAP   N6A H61A sing N N 346 
NAP   N6A H62A sing N N 347 
NAP   N1A C2A  sing Y N 348 
NAP   C2A N3A  doub Y N 349 
NAP   C2A H2A  sing N N 350 
NAP   N3A C4A  sing Y N 351 
NAP   O3  PN   sing N N 352 
NAP   PN  O1N  doub N N 353 
NAP   PN  O2N  sing N N 354 
NAP   PN  O5D  sing N N 355 
NAP   O5D C5D  sing N N 356 
NAP   C5D C4D  sing N N 357 
NAP   C5D H51N sing N N 358 
NAP   C5D H52N sing N N 359 
NAP   C4D O4D  sing N N 360 
NAP   C4D C3D  sing N N 361 
NAP   C4D H4D  sing N N 362 
NAP   O4D C1D  sing N N 363 
NAP   C3D O3D  sing N N 364 
NAP   C3D C2D  sing N N 365 
NAP   C3D H3D  sing N N 366 
NAP   O3D HO3N sing N N 367 
NAP   C2D O2D  sing N N 368 
NAP   C2D C1D  sing N N 369 
NAP   C2D H2D  sing N N 370 
NAP   O2D HO2N sing N N 371 
NAP   C1D N1N  sing N N 372 
NAP   C1D H1D  sing N N 373 
NAP   N1N C2N  sing Y N 374 
NAP   N1N C6N  doub Y N 375 
NAP   C2N C3N  doub Y N 376 
NAP   C2N H2N  sing N N 377 
NAP   C3N C7N  sing N N 378 
NAP   C3N C4N  sing Y N 379 
NAP   C7N O7N  doub N N 380 
NAP   C7N N7N  sing N N 381 
NAP   N7N H71N sing N N 382 
NAP   N7N H72N sing N N 383 
NAP   C4N C5N  doub Y N 384 
NAP   C4N H4N  sing N N 385 
NAP   C5N C6N  sing Y N 386 
NAP   C5N H5N  sing N N 387 
NAP   C6N H6N  sing N N 388 
NAP   P2B O1X  doub N N 389 
NAP   P2B O2X  sing N N 390 
NAP   P2B O3X  sing N N 391 
NAP   O2X HOP2 sing N N 392 
NAP   O3X HOP3 sing N N 393 
PHE   N   CA   sing N N 394 
PHE   N   H    sing N N 395 
PHE   N   H2   sing N N 396 
PHE   CA  C    sing N N 397 
PHE   CA  CB   sing N N 398 
PHE   CA  HA   sing N N 399 
PHE   C   O    doub N N 400 
PHE   C   OXT  sing N N 401 
PHE   CB  CG   sing N N 402 
PHE   CB  HB2  sing N N 403 
PHE   CB  HB3  sing N N 404 
PHE   CG  CD1  doub Y N 405 
PHE   CG  CD2  sing Y N 406 
PHE   CD1 CE1  sing Y N 407 
PHE   CD1 HD1  sing N N 408 
PHE   CD2 CE2  doub Y N 409 
PHE   CD2 HD2  sing N N 410 
PHE   CE1 CZ   doub Y N 411 
PHE   CE1 HE1  sing N N 412 
PHE   CE2 CZ   sing Y N 413 
PHE   CE2 HE2  sing N N 414 
PHE   CZ  HZ   sing N N 415 
PHE   OXT HXT  sing N N 416 
PRO   N   CA   sing N N 417 
PRO   N   CD   sing N N 418 
PRO   N   H    sing N N 419 
PRO   CA  C    sing N N 420 
PRO   CA  CB   sing N N 421 
PRO   CA  HA   sing N N 422 
PRO   C   O    doub N N 423 
PRO   C   OXT  sing N N 424 
PRO   CB  CG   sing N N 425 
PRO   CB  HB2  sing N N 426 
PRO   CB  HB3  sing N N 427 
PRO   CG  CD   sing N N 428 
PRO   CG  HG2  sing N N 429 
PRO   CG  HG3  sing N N 430 
PRO   CD  HD2  sing N N 431 
PRO   CD  HD3  sing N N 432 
PRO   OXT HXT  sing N N 433 
SER   N   CA   sing N N 434 
SER   N   H    sing N N 435 
SER   N   H2   sing N N 436 
SER   CA  C    sing N N 437 
SER   CA  CB   sing N N 438 
SER   CA  HA   sing N N 439 
SER   C   O    doub N N 440 
SER   C   OXT  sing N N 441 
SER   CB  OG   sing N N 442 
SER   CB  HB2  sing N N 443 
SER   CB  HB3  sing N N 444 
SER   OG  HG   sing N N 445 
SER   OXT HXT  sing N N 446 
THR   N   CA   sing N N 447 
THR   N   H    sing N N 448 
THR   N   H2   sing N N 449 
THR   CA  C    sing N N 450 
THR   CA  CB   sing N N 451 
THR   CA  HA   sing N N 452 
THR   C   O    doub N N 453 
THR   C   OXT  sing N N 454 
THR   CB  OG1  sing N N 455 
THR   CB  CG2  sing N N 456 
THR   CB  HB   sing N N 457 
THR   OG1 HG1  sing N N 458 
THR   CG2 HG21 sing N N 459 
THR   CG2 HG22 sing N N 460 
THR   CG2 HG23 sing N N 461 
THR   OXT HXT  sing N N 462 
TRP   N   CA   sing N N 463 
TRP   N   H    sing N N 464 
TRP   N   H2   sing N N 465 
TRP   CA  C    sing N N 466 
TRP   CA  CB   sing N N 467 
TRP   CA  HA   sing N N 468 
TRP   C   O    doub N N 469 
TRP   C   OXT  sing N N 470 
TRP   CB  CG   sing N N 471 
TRP   CB  HB2  sing N N 472 
TRP   CB  HB3  sing N N 473 
TRP   CG  CD1  doub Y N 474 
TRP   CG  CD2  sing Y N 475 
TRP   CD1 NE1  sing Y N 476 
TRP   CD1 HD1  sing N N 477 
TRP   CD2 CE2  doub Y N 478 
TRP   CD2 CE3  sing Y N 479 
TRP   NE1 CE2  sing Y N 480 
TRP   NE1 HE1  sing N N 481 
TRP   CE2 CZ2  sing Y N 482 
TRP   CE3 CZ3  doub Y N 483 
TRP   CE3 HE3  sing N N 484 
TRP   CZ2 CH2  doub Y N 485 
TRP   CZ2 HZ2  sing N N 486 
TRP   CZ3 CH2  sing Y N 487 
TRP   CZ3 HZ3  sing N N 488 
TRP   CH2 HH2  sing N N 489 
TRP   OXT HXT  sing N N 490 
TYR   N   CA   sing N N 491 
TYR   N   H    sing N N 492 
TYR   N   H2   sing N N 493 
TYR   CA  C    sing N N 494 
TYR   CA  CB   sing N N 495 
TYR   CA  HA   sing N N 496 
TYR   C   O    doub N N 497 
TYR   C   OXT  sing N N 498 
TYR   CB  CG   sing N N 499 
TYR   CB  HB2  sing N N 500 
TYR   CB  HB3  sing N N 501 
TYR   CG  CD1  doub Y N 502 
TYR   CG  CD2  sing Y N 503 
TYR   CD1 CE1  sing Y N 504 
TYR   CD1 HD1  sing N N 505 
TYR   CD2 CE2  doub Y N 506 
TYR   CD2 HD2  sing N N 507 
TYR   CE1 CZ   doub Y N 508 
TYR   CE1 HE1  sing N N 509 
TYR   CE2 CZ   sing Y N 510 
TYR   CE2 HE2  sing N N 511 
TYR   CZ  OH   sing N N 512 
TYR   OH  HH   sing N N 513 
TYR   OXT HXT  sing N N 514 
VAL   N   CA   sing N N 515 
VAL   N   H    sing N N 516 
VAL   N   H2   sing N N 517 
VAL   CA  C    sing N N 518 
VAL   CA  CB   sing N N 519 
VAL   CA  HA   sing N N 520 
VAL   C   O    doub N N 521 
VAL   C   OXT  sing N N 522 
VAL   CB  CG1  sing N N 523 
VAL   CB  CG2  sing N N 524 
VAL   CB  HB   sing N N 525 
VAL   CG1 HG11 sing N N 526 
VAL   CG1 HG12 sing N N 527 
VAL   CG1 HG13 sing N N 528 
VAL   CG2 HG21 sing N N 529 
VAL   CG2 HG22 sing N N 530 
VAL   CG2 HG23 sing N N 531 
VAL   OXT HXT  sing N N 532 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82173702 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2J3H 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JI7 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.011458 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011458 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.004424 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU   A 1 1   ? -15.551 -1.306  48.744  1.00 93.15  ? -2  LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 1   ? -14.234 -1.031  48.180  1.00 94.18  ? -2  LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 1   ? -13.743 0.415   48.414  1.00 102.30 ? -2  LEU   A C   1 
ATOM   4    O O   . LEU   A 1 1   ? -13.523 0.794   49.567  1.00 105.39 ? -2  LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 1   ? -14.228 -1.387  46.693  1.00 93.88  ? -2  LEU   A CB  1 
ATOM   6    C CG  . LEU   A 1 1   ? -14.422 -2.869  46.385  1.00 99.50  ? -2  LEU   A CG  1 
ATOM   7    C CD1 . LEU   A 1 1   ? -15.619 -3.422  47.144  1.00 96.85  ? -2  LEU   A CD1 1 
ATOM   8    C CD2 . LEU   A 1 1   ? -14.551 -3.114  44.888  1.00 84.74  ? -2  LEU   A CD2 1 
ATOM   9    N N   . GLY   A 1 2   ? -13.559 1.226   47.361  1.00 93.23  ? -1  GLY   A N   1 
ATOM   10   C CA  . GLY   A 1 2   ? -13.000 2.563   47.544  1.00 75.23  ? -1  GLY   A CA  1 
ATOM   11   C C   . GLY   A 1 2   ? -13.312 3.670   46.565  1.00 68.90  ? -1  GLY   A C   1 
ATOM   12   O O   . GLY   A 1 2   ? -14.262 3.563   45.798  1.00 63.64  ? -1  GLY   A O   1 
ATOM   13   N N   . SER   A 1 3   ? -12.508 4.729   46.578  1.00 53.85  ? 0   SER   A N   1 
ATOM   14   C CA  . SER   A 1 3   ? -12.774 5.884   45.745  1.00 55.00  ? 0   SER   A CA  1 
ATOM   15   C C   . SER   A 1 3   ? -11.517 6.687   45.470  1.00 55.06  ? 0   SER   A C   1 
ATOM   16   O O   . SER   A 1 3   ? -10.499 6.482   46.110  1.00 51.62  ? 0   SER   A O   1 
ATOM   17   C CB  . SER   A 1 3   ? -13.781 6.786   46.436  1.00 47.09  ? 0   SER   A CB  1 
ATOM   18   O OG  . SER   A 1 3   ? -13.129 7.691   47.300  1.00 49.47  ? 0   SER   A OG  1 
ATOM   19   N N   . MET   A 1 4   ? -11.600 7.617   44.526  1.00 49.82  ? 1   MET   A N   1 
ATOM   20   C CA  . MET   A 1 4   ? -10.459 8.443   44.230  1.00 49.11  ? 1   MET   A CA  1 
ATOM   21   C C   . MET   A 1 4   ? -10.900 9.855   43.968  1.00 48.49  ? 1   MET   A C   1 
ATOM   22   O O   . MET   A 1 4   ? -12.045 10.112  43.654  1.00 49.18  ? 1   MET   A O   1 
ATOM   23   C CB  . MET   A 1 4   ? -9.700  7.920   43.025  1.00 52.83  ? 1   MET   A CB  1 
ATOM   24   C CG  . MET   A 1 4   ? -10.413 8.014   41.698  1.00 47.42  ? 1   MET   A CG  1 
ATOM   25   S SD  . MET   A 1 4   ? -9.252  7.469   40.443  1.00 48.80  ? 1   MET   A SD  1 
ATOM   26   C CE  . MET   A 1 4   ? -7.898  8.589   40.760  1.00 33.28  ? 1   MET   A CE  1 
ATOM   27   N N   . LYS   A 1 5   ? -9.979  10.777  44.123  1.00 48.16  ? 2   LYS   A N   1 
ATOM   28   C CA  . LYS   A 1 5   ? -10.283 12.155  43.876  1.00 53.21  ? 2   LYS   A CA  1 
ATOM   29   C C   . LYS   A 1 5   ? -9.953  12.490  42.440  1.00 53.59  ? 2   LYS   A C   1 
ATOM   30   O O   . LYS   A 1 5   ? -8.890  12.145  41.948  1.00 52.47  ? 2   LYS   A O   1 
ATOM   31   C CB  . LYS   A 1 5   ? -9.498  13.043  44.839  1.00 53.35  ? 2   LYS   A CB  1 
ATOM   32   C CG  . LYS   A 1 5   ? -9.839  12.842  46.303  1.00 64.38  ? 2   LYS   A CG  1 
ATOM   33   C CD  . LYS   A 1 5   ? -11.341 12.804  46.529  1.00 70.96  ? 2   LYS   A CD  1 
ATOM   34   C CE  . LYS   A 1 5   ? -11.707 11.820  47.630  1.00 75.01  ? 2   LYS   A CE  1 
ATOM   35   N NZ  . LYS   A 1 5   ? -12.237 10.540  47.085  1.00 72.75  ? 2   LYS   A NZ  1 
ATOM   36   N N   . THR   A 1 6   ? -10.865 13.163  41.766  1.00 44.27  ? 3   THR   A N   1 
ATOM   37   C CA  . THR   A 1 6   ? -10.658 13.507  40.393  1.00 46.78  ? 3   THR   A CA  1 
ATOM   38   C C   . THR   A 1 6   ? -11.055 14.927  40.140  1.00 50.06  ? 3   THR   A C   1 
ATOM   39   O O   . THR   A 1 6   ? -11.792 15.503  40.910  1.00 59.20  ? 3   THR   A O   1 
ATOM   40   C CB  . THR   A 1 6   ? -11.535 12.632  39.488  1.00 48.03  ? 3   THR   A CB  1 
ATOM   41   O OG1 . THR   A 1 6   ? -12.909 12.989  39.665  1.00 45.05  ? 3   THR   A OG1 1 
ATOM   42   C CG2 . THR   A 1 6   ? -11.350 11.164  39.815  1.00 44.37  ? 3   THR   A CG2 1 
ATOM   43   N N   . GLU   A 1 7   ? -10.561 15.515  39.068  1.00 52.26  ? 4   GLU   A N   1 
ATOM   44   C CA  . GLU   A 1 7   ? -11.003 16.844  38.683  1.00 49.50  ? 4   GLU   A CA  1 
ATOM   45   C C   . GLU   A 1 7   ? -11.748 16.777  37.356  1.00 48.06  ? 4   GLU   A C   1 
ATOM   46   O O   . GLU   A 1 7   ? -11.434 15.964  36.477  1.00 47.18  ? 4   GLU   A O   1 
ATOM   47   C CB  . GLU   A 1 7   ? -9.828  17.818  38.586  1.00 48.26  ? 4   GLU   A CB  1 
ATOM   48   C CG  . GLU   A 1 7   ? -9.339  18.316  39.936  1.00 52.07  ? 4   GLU   A CG  1 
ATOM   49   C CD  . GLU   A 1 7   ? -8.154  19.264  39.801  1.00 60.95  ? 4   GLU   A CD  1 
ATOM   50   O OE1 . GLU   A 1 7   ? -7.085  18.822  39.321  1.00 66.49  ? 4   GLU   A OE1 1 
ATOM   51   O OE2 . GLU   A 1 7   ? -8.293  20.455  40.158  1.00 58.08  ? 4   GLU   A OE2 1 
ATOM   52   N N   . ARG   A 1 8   ? -12.755 17.631  37.223  1.00 46.29  ? 5   ARG   A N   1 
ATOM   53   C CA  . ARG   A 1 8   ? -13.583 17.666  36.033  1.00 42.67  ? 5   ARG   A CA  1 
ATOM   54   C C   . ARG   A 1 8   ? -13.860 19.113  35.665  1.00 45.87  ? 5   ARG   A C   1 
ATOM   55   O O   . ARG   A 1 8   ? -14.012 19.966  36.543  1.00 46.28  ? 5   ARG   A O   1 
ATOM   56   C CB  . ARG   A 1 8   ? -14.897 16.922  36.263  1.00 41.16  ? 5   ARG   A CB  1 
ATOM   57   C CG  . ARG   A 1 8   ? -14.708 15.504  36.775  1.00 43.86  ? 5   ARG   A CG  1 
ATOM   58   C CD  . ARG   A 1 8   ? -16.035 14.792  36.847  1.00 45.17  ? 5   ARG   A CD  1 
ATOM   59   N NE  . ARG   A 1 8   ? -17.000 15.590  37.593  1.00 50.77  ? 5   ARG   A NE  1 
ATOM   60   C CZ  . ARG   A 1 8   ? -18.291 15.648  37.304  1.00 50.69  ? 5   ARG   A CZ  1 
ATOM   61   N NH1 . ARG   A 1 8   ? -18.795 14.980  36.280  1.00 45.74  ? 5   ARG   A NH1 1 
ATOM   62   N NH2 . ARG   A 1 8   ? -19.090 16.408  38.050  1.00 44.79  ? 5   ARG   A NH2 1 
ATOM   63   N N   . TRP   A 1 9   ? -13.897 19.395  34.368  1.00 41.68  ? 6   TRP   A N   1 
ATOM   64   C CA  . TRP   A 1 9   ? -14.480 20.642  33.881  1.00 42.32  ? 6   TRP   A CA  1 
ATOM   65   C C   . TRP   A 1 9   ? -15.937 20.374  33.533  1.00 42.16  ? 6   TRP   A C   1 
ATOM   66   O O   . TRP   A 1 9   ? -16.251 19.407  32.831  1.00 40.08  ? 6   TRP   A O   1 
ATOM   67   C CB  . TRP   A 1 9   ? -13.730 21.180  32.670  1.00 41.14  ? 6   TRP   A CB  1 
ATOM   68   C CG  . TRP   A 1 9   ? -12.399 21.756  32.992  1.00 38.86  ? 6   TRP   A CG  1 
ATOM   69   C CD1 . TRP   A 1 9   ? -11.182 21.134  32.889  1.00 37.76  ? 6   TRP   A CD1 1 
ATOM   70   C CD2 . TRP   A 1 9   ? -12.134 23.083  33.453  1.00 34.37  ? 6   TRP   A CD2 1 
ATOM   71   N NE1 . TRP   A 1 9   ? -10.175 21.999  33.265  1.00 36.78  ? 6   TRP   A NE1 1 
ATOM   72   C CE2 . TRP   A 1 9   ? -10.737 23.201  33.616  1.00 36.23  ? 6   TRP   A CE2 1 
ATOM   73   C CE3 . TRP   A 1 9   ? -12.942 24.182  33.748  1.00 38.56  ? 6   TRP   A CE3 1 
ATOM   74   C CZ2 . TRP   A 1 9   ? -10.135 24.380  34.050  1.00 39.28  ? 6   TRP   A CZ2 1 
ATOM   75   C CZ3 . TRP   A 1 9   ? -12.346 25.342  34.195  1.00 39.32  ? 6   TRP   A CZ3 1 
ATOM   76   C CH2 . TRP   A 1 9   ? -10.955 25.438  34.332  1.00 34.75  ? 6   TRP   A CH2 1 
ATOM   77   N N   . VAL   A 1 10  ? -16.831 21.205  34.058  1.00 50.00  ? 7   VAL   A N   1 
ATOM   78   C CA  . VAL   A 1 10  ? -18.258 20.969  33.915  1.00 46.45  ? 7   VAL   A CA  1 
ATOM   79   C C   . VAL   A 1 10  ? -18.893 22.196  33.291  1.00 44.56  ? 7   VAL   A C   1 
ATOM   80   O O   . VAL   A 1 10  ? -18.356 23.305  33.352  1.00 47.36  ? 7   VAL   A O   1 
ATOM   81   C CB  . VAL   A 1 10  ? -18.941 20.634  35.258  1.00 51.07  ? 7   VAL   A CB  1 
ATOM   82   C CG1 . VAL   A 1 10  ? -18.379 19.341  35.827  1.00 49.24  ? 7   VAL   A CG1 1 
ATOM   83   C CG2 . VAL   A 1 10  ? -18.765 21.784  36.247  1.00 51.89  ? 7   VAL   A CG2 1 
ATOM   84   N N   . VAL   A 1 11  ? -20.064 21.981  32.699  1.00 48.21  ? 8   VAL   A N   1 
ATOM   85   C CA  . VAL   A 1 11  ? -20.771 23.038  31.989  1.00 53.39  ? 8   VAL   A CA  1 
ATOM   86   C C   . VAL   A 1 11  ? -21.547 23.870  33.003  1.00 53.60  ? 8   VAL   A C   1 
ATOM   87   O O   . VAL   A 1 11  ? -22.576 23.438  33.530  1.00 53.40  ? 8   VAL   A O   1 
ATOM   88   C CB  . VAL   A 1 11  ? -21.693 22.478  30.906  1.00 49.65  ? 8   VAL   A CB  1 
ATOM   89   C CG1 . VAL   A 1 11  ? -22.485 23.613  30.284  1.00 46.49  ? 8   VAL   A CG1 1 
ATOM   90   C CG2 . VAL   A 1 11  ? -20.871 21.754  29.857  1.00 46.36  ? 8   VAL   A CG2 1 
ATOM   91   N N   . ARG   A 1 12  ? -21.054 25.084  33.257  1.00 51.98  ? 9   ARG   A N   1 
ATOM   92   C CA  . ARG   A 1 12  ? -21.706 26.011  34.176  1.00 57.65  ? 9   ARG   A CA  1 
ATOM   93   C C   . ARG   A 1 12  ? -22.893 26.712  33.517  1.00 58.34  ? 9   ARG   A C   1 
ATOM   94   O O   . ARG   A 1 12  ? -23.970 26.805  34.113  1.00 55.46  ? 9   ARG   A O   1 
ATOM   95   C CB  . ARG   A 1 12  ? -20.672 27.025  34.681  1.00 53.75  ? 9   ARG   A CB  1 
ATOM   96   C CG  . ARG   A 1 12  ? -21.156 28.036  35.698  1.00 58.56  ? 9   ARG   A CG  1 
ATOM   97   C CD  . ARG   A 1 12  ? -19.955 28.628  36.464  1.00 67.45  ? 9   ARG   A CD  1 
ATOM   98   N NE  . ARG   A 1 12  ? -18.918 29.156  35.577  1.00 65.68  ? 9   ARG   A NE  1 
ATOM   99   C CZ  . ARG   A 1 12  ? -17.694 29.498  35.965  1.00 59.57  ? 9   ARG   A CZ  1 
ATOM   100  N NH1 . ARG   A 1 12  ? -17.301 29.352  37.218  1.00 60.95  ? 9   ARG   A NH1 1 
ATOM   101  N NH2 . ARG   A 1 12  ? -16.842 29.999  35.073  1.00 56.77  ? 9   ARG   A NH2 1 
ATOM   102  N N   . GLU   A 1 13  ? -22.726 27.192  32.282  1.00 54.91  ? 10  GLU   A N   1 
ATOM   103  C CA  . GLU   A 1 13  ? -23.724 28.066  31.682  1.00 53.27  ? 10  GLU   A CA  1 
ATOM   104  C C   . GLU   A 1 13  ? -23.717 27.911  30.165  1.00 56.13  ? 10  GLU   A C   1 
ATOM   105  O O   . GLU   A 1 13  ? -22.661 27.741  29.546  1.00 57.91  ? 10  GLU   A O   1 
ATOM   106  C CB  . GLU   A 1 13  ? -23.456 29.521  32.082  1.00 52.89  ? 10  GLU   A CB  1 
ATOM   107  C CG  . GLU   A 1 13  ? -24.619 30.474  31.872  1.00 54.54  ? 10  GLU   A CG  1 
ATOM   108  C CD  . GLU   A 1 13  ? -24.162 31.918  31.693  1.00 59.87  ? 10  GLU   A CD  1 
ATOM   109  O OE1 . GLU   A 1 13  ? -23.101 32.292  32.243  1.00 61.56  ? 10  GLU   A OE1 1 
ATOM   110  O OE2 . GLU   A 1 13  ? -24.856 32.679  30.980  1.00 63.56  ? 10  GLU   A OE2 1 
ATOM   111  N N   . HIS   A 1 14  ? -24.906 27.984  29.571  1.00 53.76  ? 11  HIS   A N   1 
ATOM   112  C CA  . HIS   A 1 14  ? -25.077 27.885  28.125  1.00 51.80  ? 11  HIS   A CA  1 
ATOM   113  C C   . HIS   A 1 14  ? -25.064 29.272  27.490  1.00 54.32  ? 11  HIS   A C   1 
ATOM   114  O O   . HIS   A 1 14  ? -25.905 30.111  27.821  1.00 58.14  ? 11  HIS   A O   1 
ATOM   115  C CB  . HIS   A 1 14  ? -26.389 27.182  27.801  1.00 43.77  ? 11  HIS   A CB  1 
ATOM   116  C CG  . HIS   A 1 14  ? -26.367 25.715  28.073  1.00 52.32  ? 11  HIS   A CG  1 
ATOM   117  N ND1 . HIS   A 1 14  ? -27.515 24.979  28.287  1.00 52.25  ? 11  HIS   A ND1 1 
ATOM   118  C CD2 . HIS   A 1 14  ? -25.336 24.839  28.148  1.00 51.22  ? 11  HIS   A CD2 1 
ATOM   119  C CE1 . HIS   A 1 14  ? -27.192 23.714  28.484  1.00 52.70  ? 11  HIS   A CE1 1 
ATOM   120  N NE2 . HIS   A 1 14  ? -25.876 23.602  28.410  1.00 52.75  ? 11  HIS   A NE2 1 
ATOM   121  N N   . VAL   A 1 15  ? -24.121 29.508  26.575  1.00 52.54  ? 12  VAL   A N   1 
ATOM   122  C CA  . VAL   A 1 15  ? -24.038 30.762  25.826  1.00 52.87  ? 12  VAL   A CA  1 
ATOM   123  C C   . VAL   A 1 15  ? -23.756 30.439  24.365  1.00 57.15  ? 12  VAL   A C   1 
ATOM   124  O O   . VAL   A 1 15  ? -22.701 29.877  24.039  1.00 57.79  ? 12  VAL   A O   1 
ATOM   125  C CB  . VAL   A 1 15  ? -22.945 31.711  26.354  1.00 60.96  ? 12  VAL   A CB  1 
ATOM   126  C CG1 . VAL   A 1 15  ? -23.105 33.092  25.718  1.00 59.04  ? 12  VAL   A CG1 1 
ATOM   127  C CG2 . VAL   A 1 15  ? -22.958 31.791  27.883  1.00 57.86  ? 12  VAL   A CG2 1 
ATOM   128  N N   . GLU   A 1 16  ? -24.669 30.833  23.481  1.00 58.90  ? 13  GLU   A N   1 
ATOM   129  C CA  . GLU   A 1 16  ? -24.507 30.570  22.062  1.00 48.39  ? 13  GLU   A CA  1 
ATOM   130  C C   . GLU   A 1 16  ? -23.433 31.472  21.454  1.00 52.27  ? 13  GLU   A C   1 
ATOM   131  O O   . GLU   A 1 16  ? -22.829 32.326  22.117  1.00 50.28  ? 13  GLU   A O   1 
ATOM   132  C CB  . GLU   A 1 16  ? -25.832 30.756  21.339  1.00 48.24  ? 13  GLU   A CB  1 
ATOM   133  C CG  . GLU   A 1 16  ? -26.876 29.795  21.807  1.00 51.48  ? 13  GLU   A CG  1 
ATOM   134  C CD  . GLU   A 1 16  ? -27.719 29.290  20.672  1.00 66.67  ? 13  GLU   A CD  1 
ATOM   135  O OE1 . GLU   A 1 16  ? -27.145 28.885  19.623  1.00 70.22  ? 13  GLU   A OE1 1 
ATOM   136  O OE2 . GLU   A 1 16  ? -28.961 29.314  20.824  1.00 73.76  ? 13  GLU   A OE2 1 
ATOM   137  N N   . GLY   A 1 17  ? -23.201 31.266  20.157  1.00 53.90  ? 14  GLY   A N   1 
ATOM   138  C CA  . GLY   A 1 17  ? -22.232 32.064  19.443  1.00 45.34  ? 14  GLY   A CA  1 
ATOM   139  C C   . GLY   A 1 17  ? -20.824 31.642  19.801  1.00 45.34  ? 14  GLY   A C   1 
ATOM   140  O O   . GLY   A 1 17  ? -20.553 30.476  20.091  1.00 48.53  ? 14  GLY   A O   1 
ATOM   141  N N   . VAL   A 1 18  ? -19.913 32.607  19.764  1.00 43.42  ? 15  VAL   A N   1 
ATOM   142  C CA  . VAL   A 1 18  ? -18.525 32.314  20.107  1.00 45.24  ? 15  VAL   A CA  1 
ATOM   143  C C   . VAL   A 1 18  ? -18.504 32.035  21.602  1.00 54.30  ? 15  VAL   A C   1 
ATOM   144  O O   . VAL   A 1 18  ? -18.995 32.863  22.386  1.00 56.83  ? 15  VAL   A O   1 
ATOM   145  C CB  . VAL   A 1 18  ? -17.579 33.461  19.731  1.00 45.32  ? 15  VAL   A CB  1 
ATOM   146  C CG1 . VAL   A 1 18  ? -16.223 33.243  20.387  1.00 51.65  ? 15  VAL   A CG1 1 
ATOM   147  C CG2 . VAL   A 1 18  ? -17.417 33.556  18.220  1.00 37.75  ? 15  VAL   A CG2 1 
ATOM   148  N N   . PRO   A 1 19  ? -18.015 30.882  22.044  1.00 56.86  ? 16  PRO   A N   1 
ATOM   149  C CA  . PRO   A 1 19  ? -18.076 30.570  23.472  1.00 51.86  ? 16  PRO   A CA  1 
ATOM   150  C C   . PRO   A 1 19  ? -17.025 31.346  24.254  1.00 57.45  ? 16  PRO   A C   1 
ATOM   151  O O   . PRO   A 1 19  ? -15.966 31.730  23.736  1.00 50.35  ? 16  PRO   A O   1 
ATOM   152  C CB  . PRO   A 1 19  ? -17.807 29.061  23.514  1.00 49.34  ? 16  PRO   A CB  1 
ATOM   153  C CG  . PRO   A 1 19  ? -16.957 28.813  22.311  1.00 50.96  ? 16  PRO   A CG  1 
ATOM   154  C CD  . PRO   A 1 19  ? -17.444 29.776  21.253  1.00 50.51  ? 16  PRO   A CD  1 
ATOM   155  N N   . ASP   A 1 20  ? -17.355 31.587  25.520  1.00 54.86  ? 17  ASP   A N   1 
ATOM   156  C CA  . ASP   A 1 20  ? -16.464 32.201  26.493  1.00 52.62  ? 17  ASP   A CA  1 
ATOM   157  C C   . ASP   A 1 20  ? -16.075 31.083  27.460  1.00 53.23  ? 17  ASP   A C   1 
ATOM   158  O O   . ASP   A 1 20  ? -16.888 30.648  28.288  1.00 51.97  ? 17  ASP   A O   1 
ATOM   159  C CB  . ASP   A 1 20  ? -17.166 33.376  27.186  1.00 55.79  ? 17  ASP   A CB  1 
ATOM   160  C CG  . ASP   A 1 20  ? -16.269 34.143  28.172  1.00 56.99  ? 17  ASP   A CG  1 
ATOM   161  O OD1 . ASP   A 1 20  ? -15.098 33.751  28.416  1.00 52.41  ? 17  ASP   A OD1 1 
ATOM   162  O OD2 . ASP   A 1 20  ? -16.760 35.156  28.712  1.00 59.70  ? 17  ASP   A OD2 1 
ATOM   163  N N   . ALA   A 1 21  ? -14.838 30.588  27.326  1.00 48.96  ? 18  ALA   A N   1 
ATOM   164  C CA  . ALA   A 1 21  ? -14.429 29.419  28.099  1.00 52.76  ? 18  ALA   A CA  1 
ATOM   165  C C   . ALA   A 1 21  ? -14.405 29.724  29.594  1.00 52.74  ? 18  ALA   A C   1 
ATOM   166  O O   . ALA   A 1 21  ? -14.845 28.903  30.412  1.00 52.46  ? 18  ALA   A O   1 
ATOM   167  C CB  . ALA   A 1 21  ? -13.068 28.922  27.618  1.00 45.62  ? 18  ALA   A CB  1 
ATOM   168  N N   . ALA   A 1 22  ? -13.904 30.906  29.969  1.00 48.51  ? 19  ALA   A N   1 
ATOM   169  C CA  . ALA   A 1 22  ? -13.851 31.284  31.382  1.00 49.16  ? 19  ALA   A CA  1 
ATOM   170  C C   . ALA   A 1 22  ? -15.238 31.319  32.014  1.00 53.70  ? 19  ALA   A C   1 
ATOM   171  O O   . ALA   A 1 22  ? -15.383 31.054  33.213  1.00 56.33  ? 19  ALA   A O   1 
ATOM   172  C CB  . ALA   A 1 22  ? -13.174 32.642  31.537  1.00 50.27  ? 19  ALA   A CB  1 
ATOM   173  N N   . ARG   A 1 23  ? -16.265 31.626  31.226  1.00 52.25  ? 20  ARG   A N   1 
ATOM   174  C CA  . ARG   A 1 23  ? -17.611 31.769  31.753  1.00 52.13  ? 20  ARG   A CA  1 
ATOM   175  C C   . ARG   A 1 23  ? -18.411 30.474  31.722  1.00 54.08  ? 20  ARG   A C   1 
ATOM   176  O O   . ARG   A 1 23  ? -19.206 30.228  32.637  1.00 54.86  ? 20  ARG   A O   1 
ATOM   177  C CB  . ARG   A 1 23  ? -18.338 32.851  30.962  1.00 50.35  ? 20  ARG   A CB  1 
ATOM   178  C CG  . ARG   A 1 23  ? -19.784 33.024  31.295  1.00 53.04  ? 20  ARG   A CG  1 
ATOM   179  C CD  . ARG   A 1 23  ? -20.325 34.102  30.405  1.00 55.26  ? 20  ARG   A CD  1 
ATOM   180  N NE  . ARG   A 1 23  ? -21.747 34.318  30.605  1.00 52.56  ? 20  ARG   A NE  1 
ATOM   181  C CZ  . ARG   A 1 23  ? -22.484 35.085  29.817  1.00 58.65  ? 20  ARG   A CZ  1 
ATOM   182  N NH1 . ARG   A 1 23  ? -21.966 35.665  28.742  1.00 53.20  ? 20  ARG   A NH1 1 
ATOM   183  N NH2 . ARG   A 1 23  ? -23.769 35.276  30.115  1.00 56.19  ? 20  ARG   A NH2 1 
ATOM   184  N N   . ILE   A 1 24  ? -18.209 29.635  30.702  1.00 58.08  ? 21  ILE   A N   1 
ATOM   185  C CA  . ILE   A 1 24  ? -19.046 28.449  30.503  1.00 55.33  ? 21  ILE   A CA  1 
ATOM   186  C C   . ILE   A 1 24  ? -18.574 27.277  31.364  1.00 49.61  ? 21  ILE   A C   1 
ATOM   187  O O   . ILE   A 1 24  ? -19.380 26.424  31.754  1.00 50.11  ? 21  ILE   A O   1 
ATOM   188  C CB  . ILE   A 1 24  ? -19.075 28.084  29.001  1.00 54.24  ? 21  ILE   A CB  1 
ATOM   189  C CG1 . ILE   A 1 24  ? -19.787 29.184  28.200  1.00 58.22  ? 21  ILE   A CG1 1 
ATOM   190  C CG2 . ILE   A 1 24  ? -19.735 26.725  28.754  1.00 48.24  ? 21  ILE   A CG2 1 
ATOM   191  C CD1 . ILE   A 1 24  ? -19.647 29.064  26.681  1.00 55.51  ? 21  ILE   A CD1 1 
ATOM   192  N N   . TYR   A 1 25  ? -17.287 27.217  31.692  1.00 50.59  ? 22  TYR   A N   1 
ATOM   193  C CA  . TYR   A 1 25  ? -16.704 26.030  32.301  1.00 51.85  ? 22  TYR   A CA  1 
ATOM   194  C C   . TYR   A 1 25  ? -16.180 26.317  33.707  1.00 55.20  ? 22  TYR   A C   1 
ATOM   195  O O   . TYR   A 1 25  ? -15.700 27.416  34.015  1.00 52.08  ? 22  TYR   A O   1 
ATOM   196  C CB  . TYR   A 1 25  ? -15.582 25.459  31.402  1.00 43.47  ? 22  TYR   A CB  1 
ATOM   197  C CG  . TYR   A 1 25  ? -16.113 24.978  30.080  1.00 46.92  ? 22  TYR   A CG  1 
ATOM   198  C CD1 . TYR   A 1 25  ? -16.949 23.876  30.012  1.00 48.74  ? 22  TYR   A CD1 1 
ATOM   199  C CD2 . TYR   A 1 25  ? -15.806 25.636  28.901  1.00 45.26  ? 22  TYR   A CD2 1 
ATOM   200  C CE1 . TYR   A 1 25  ? -17.457 23.432  28.802  1.00 45.36  ? 22  TYR   A CE1 1 
ATOM   201  C CE2 . TYR   A 1 25  ? -16.313 25.198  27.689  1.00 43.26  ? 22  TYR   A CE2 1 
ATOM   202  C CZ  . TYR   A 1 25  ? -17.136 24.097  27.650  1.00 43.58  ? 22  TYR   A CZ  1 
ATOM   203  O OH  . TYR   A 1 25  ? -17.645 23.648  26.451  1.00 46.94  ? 22  TYR   A OH  1 
ATOM   204  N N   . GLU   A 1 26  ? -16.263 25.296  34.555  1.00 55.37  ? 23  GLU   A N   1 
ATOM   205  C CA  . GLU   A 1 26  ? -15.861 25.400  35.951  1.00 57.72  ? 23  GLU   A CA  1 
ATOM   206  C C   . GLU   A 1 26  ? -15.163 24.103  36.343  1.00 53.53  ? 23  GLU   A C   1 
ATOM   207  O O   . GLU   A 1 26  ? -15.659 23.017  36.023  1.00 52.98  ? 23  GLU   A O   1 
ATOM   208  C CB  . GLU   A 1 26  ? -17.096 25.675  36.825  1.00 57.99  ? 23  GLU   A CB  1 
ATOM   209  C CG  . GLU   A 1 26  ? -17.011 25.230  38.273  1.00 66.82  ? 23  GLU   A CG  1 
ATOM   210  C CD  . GLU   A 1 26  ? -18.238 25.649  39.077  1.00 74.57  ? 23  GLU   A CD  1 
ATOM   211  O OE1 . GLU   A 1 26  ? -19.348 25.097  38.839  1.00 70.04  ? 23  GLU   A OE1 1 
ATOM   212  O OE2 . GLU   A 1 26  ? -18.083 26.551  39.934  1.00 76.89  ? 23  GLU   A OE2 1 
ATOM   213  N N   . LYS   A 1 27  ? -14.004 24.211  37.001  1.00 43.97  ? 24  LYS   A N   1 
ATOM   214  C CA  . LYS   A 1 27  ? -13.238 23.035  37.406  1.00 42.94  ? 24  LYS   A CA  1 
ATOM   215  C C   . LYS   A 1 27  ? -13.636 22.618  38.821  1.00 51.80  ? 24  LYS   A C   1 
ATOM   216  O O   . LYS   A 1 27  ? -13.284 23.285  39.801  1.00 54.10  ? 24  LYS   A O   1 
ATOM   217  C CB  . LYS   A 1 27  ? -11.743 23.312  37.328  1.00 42.59  ? 24  LYS   A CB  1 
ATOM   218  C CG  . LYS   A 1 27  ? -10.900 22.047  37.303  1.00 43.62  ? 24  LYS   A CG  1 
ATOM   219  C CD  . LYS   A 1 27  ? -9.418  22.386  37.323  1.00 47.11  ? 24  LYS   A CD  1 
ATOM   220  C CE  . LYS   A 1 27  ? -9.059  23.126  38.602  1.00 46.42  ? 24  LYS   A CE  1 
ATOM   221  N NZ  . LYS   A 1 27  ? -7.598  23.151  38.817  1.00 50.02  ? 24  LYS   A NZ  1 
ATOM   222  N N   . VAL   A 1 28  ? -14.298 21.480  38.912  1.00 49.64  ? 25  VAL   A N   1 
ATOM   223  C CA  . VAL   A 1 28  ? -14.727 20.959  40.191  1.00 49.87  ? 25  VAL   A CA  1 
ATOM   224  C C   . VAL   A 1 28  ? -13.935 19.734  40.607  1.00 54.48  ? 25  VAL   A C   1 
ATOM   225  O O   . VAL   A 1 28  ? -13.373 19.044  39.769  1.00 50.81  ? 25  VAL   A O   1 
ATOM   226  C CB  . VAL   A 1 28  ? -16.202 20.561  40.117  1.00 46.37  ? 25  VAL   A CB  1 
ATOM   227  C CG1 . VAL   A 1 28  ? -17.013 21.680  39.494  1.00 49.34  ? 25  VAL   A CG1 1 
ATOM   228  C CG2 . VAL   A 1 28  ? -16.371 19.277  39.323  1.00 45.89  ? 25  VAL   A CG2 1 
ATOM   229  N N   . GLU   A 1 29  ? -13.871 19.472  41.903  1.00 54.52  ? 26  GLU   A N   1 
ATOM   230  C CA  . GLU   A 1 29  ? -13.213 18.269  42.389  1.00 59.72  ? 26  GLU   A CA  1 
ATOM   231  C C   . GLU   A 1 29  ? -14.272 17.214  42.585  1.00 56.71  ? 26  GLU   A C   1 
ATOM   232  O O   . GLU   A 1 29  ? -15.332 17.500  43.105  1.00 55.28  ? 26  GLU   A O   1 
ATOM   233  C CB  . GLU   A 1 29  ? -12.453 18.533  43.680  1.00 60.50  ? 26  GLU   A CB  1 
ATOM   234  C CG  . GLU   A 1 29  ? -11.260 19.457  43.511  1.00 71.71  ? 26  GLU   A CG  1 
ATOM   235  C CD  . GLU   A 1 29  ? -10.568 19.758  44.826  1.00 84.73  ? 26  GLU   A CD  1 
ATOM   236  O OE1 . GLU   A 1 29  ? -11.124 19.405  45.886  1.00 79.77  ? 26  GLU   A OE1 1 
ATOM   237  O OE2 . GLU   A 1 29  ? -9.468  20.347  44.799  1.00 81.91  ? 26  GLU   A OE2 1 
ATOM   238  N N   . THR   A 1 30  ? -13.998 15.996  42.158  1.00 54.46  ? 27  THR   A N   1 
ATOM   239  C CA  . THR   A 1 30  ? -15.014 14.967  42.203  1.00 54.46  ? 27  THR   A CA  1 
ATOM   240  C C   . THR   A 1 30  ? -14.481 13.645  42.709  1.00 54.74  ? 27  THR   A C   1 
ATOM   241  O O   . THR   A 1 30  ? -13.368 13.258  42.408  1.00 56.23  ? 27  THR   A O   1 
ATOM   242  C CB  . THR   A 1 30  ? -15.650 14.794  40.808  1.00 52.08  ? 27  THR   A CB  1 
ATOM   243  O OG1 . THR   A 1 30  ? -16.369 15.980  40.464  1.00 56.78  ? 27  THR   A OG1 1 
ATOM   244  C CG2 . THR   A 1 30  ? -16.604 13.623  40.783  1.00 47.43  ? 27  THR   A CG2 1 
ATOM   245  N N   . GLU   A 1 31  ? -15.289 12.948  43.486  1.00 54.44  ? 28  GLU   A N   1 
ATOM   246  C CA  . GLU   A 1 31  ? -14.881 11.686  44.031  1.00 52.96  ? 28  GLU   A CA  1 
ATOM   247  C C   . GLU   A 1 31  ? -15.398 10.604  43.172  1.00 52.90  ? 28  GLU   A C   1 
ATOM   248  O O   . GLU   A 1 31  ? -16.591 10.517  42.930  1.00 53.84  ? 28  GLU   A O   1 
ATOM   249  C CB  . GLU   A 1 31  ? -15.441 11.515  45.423  1.00 57.67  ? 28  GLU   A CB  1 
ATOM   250  C CG  . GLU   A 1 31  ? -14.859 12.482  46.438  1.00 63.82  ? 28  GLU   A CG  1 
ATOM   251  C CD  . GLU   A 1 31  ? -15.490 12.336  47.807  1.00 72.49  ? 28  GLU   A CD  1 
ATOM   252  O OE1 . GLU   A 1 31  ? -16.506 11.619  47.923  1.00 71.39  ? 28  GLU   A OE1 1 
ATOM   253  O OE2 . GLU   A 1 31  ? -14.970 12.941  48.766  1.00 72.96  ? 28  GLU   A OE2 1 
ATOM   254  N N   . LEU   A 1 32  ? -14.499 9.756   42.719  1.00 48.81  ? 29  LEU   A N   1 
ATOM   255  C CA  . LEU   A 1 32  ? -14.904 8.730   41.804  1.00 49.51  ? 29  LEU   A CA  1 
ATOM   256  C C   . LEU   A 1 32  ? -14.868 7.409   42.468  1.00 50.34  ? 29  LEU   A C   1 
ATOM   257  O O   . LEU   A 1 32  ? -13.894 7.041   43.096  1.00 52.82  ? 29  LEU   A O   1 
ATOM   258  C CB  . LEU   A 1 32  ? -14.008 8.713   40.560  1.00 47.70  ? 29  LEU   A CB  1 
ATOM   259  C CG  . LEU   A 1 32  ? -14.277 7.679   39.478  1.00 45.88  ? 29  LEU   A CG  1 
ATOM   260  C CD1 . LEU   A 1 32  ? -15.702 7.821   38.981  1.00 42.73  ? 29  LEU   A CD1 1 
ATOM   261  C CD2 . LEU   A 1 32  ? -13.293 7.871   38.342  1.00 38.65  ? 29  LEU   A CD2 1 
ATOM   262  N N   . ASN   A 1 33  ? -15.956 6.696   42.339  1.00 48.66  ? 30  ASN   A N   1 
ATOM   263  C CA  . ASN   A 1 33  ? -16.004 5.352   42.874  1.00 50.92  ? 30  ASN   A CA  1 
ATOM   264  C C   . ASN   A 1 33  ? -15.166 4.424   42.012  1.00 52.20  ? 30  ASN   A C   1 
ATOM   265  O O   . ASN   A 1 33  ? -15.352 4.365   40.793  1.00 54.68  ? 30  ASN   A O   1 
ATOM   266  C CB  . ASN   A 1 33  ? -17.431 4.834   42.923  1.00 54.22  ? 30  ASN   A CB  1 
ATOM   267  C CG  . ASN   A 1 33  ? -17.472 3.379   43.304  1.00 60.83  ? 30  ASN   A CG  1 
ATOM   268  O OD1 . ASN   A 1 33  ? -16.858 2.990   44.301  1.00 65.13  ? 30  ASN   A OD1 1 
ATOM   269  N ND2 . ASN   A 1 33  ? -18.130 2.553   42.489  1.00 61.50  ? 30  ASN   A ND2 1 
ATOM   270  N N   . THR   A 1 34  ? -14.271 3.675   42.641  1.00 51.61  ? 31  THR   A N   1 
ATOM   271  C CA  . THR   A 1 34  ? -13.397 2.772   41.911  1.00 54.70  ? 31  THR   A CA  1 
ATOM   272  C C   . THR   A 1 34  ? -13.891 1.320   41.908  1.00 55.15  ? 31  THR   A C   1 
ATOM   273  O O   . THR   A 1 34  ? -13.138 0.421   41.519  1.00 55.69  ? 31  THR   A O   1 
ATOM   274  C CB  . THR   A 1 34  ? -11.968 2.881   42.464  1.00 53.15  ? 31  THR   A CB  1 
ATOM   275  O OG1 . THR   A 1 34  ? -11.946 2.504   43.840  1.00 57.90  ? 31  THR   A OG1 1 
ATOM   276  C CG2 . THR   A 1 34  ? -11.478 4.314   42.359  1.00 47.45  ? 31  THR   A CG2 1 
ATOM   277  N N   . ARG   A 1 35  ? -15.144 1.073   42.298  1.00 56.45  ? 32  ARG   A N   1 
ATOM   278  C CA  . ARG   A 1 35  ? -15.743 -0.254  42.178  1.00 54.85  ? 32  ARG   A CA  1 
ATOM   279  C C   . ARG   A 1 35  ? -16.124 -0.516  40.728  1.00 52.46  ? 32  ARG   A C   1 
ATOM   280  O O   . ARG   A 1 35  ? -16.875 0.261   40.128  1.00 55.53  ? 32  ARG   A O   1 
ATOM   281  C CB  . ARG   A 1 35  ? -16.997 -0.375  43.048  1.00 68.73  ? 32  ARG   A CB  1 
ATOM   282  C CG  . ARG   A 1 35  ? -16.828 -0.174  44.553  1.00 76.55  ? 32  ARG   A CG  1 
ATOM   283  C CD  . ARG   A 1 35  ? -18.136 0.369   45.147  1.00 82.57  ? 32  ARG   A CD  1 
ATOM   284  N NE  . ARG   A 1 35  ? -18.416 -0.103  46.499  1.00 91.69  ? 32  ARG   A NE  1 
ATOM   285  C CZ  . ARG   A 1 35  ? -19.080 -1.219  46.776  1.00 93.84  ? 32  ARG   A CZ  1 
ATOM   286  N NH1 . ARG   A 1 35  ? -19.514 -2.021  45.814  1.00 88.94  ? 32  ARG   A NH1 1 
ATOM   287  N NH2 . ARG   A 1 35  ? -19.307 -1.543  48.048  1.00 88.14  ? 32  ARG   A NH2 1 
ATOM   288  N N   . LEU   A 1 36  ? -15.646 -1.623  40.173  1.00 46.83  ? 33  LEU   A N   1 
ATOM   289  C CA  . LEU   A 1 36  ? -15.777 -1.888  38.746  1.00 49.28  ? 33  LEU   A CA  1 
ATOM   290  C C   . LEU   A 1 36  ? -16.729 -3.057  38.487  1.00 51.91  ? 33  LEU   A C   1 
ATOM   291  O O   . LEU   A 1 36  ? -16.546 -4.160  39.028  1.00 48.13  ? 33  LEU   A O   1 
ATOM   292  C CB  . LEU   A 1 36  ? -14.401 -2.160  38.124  1.00 45.79  ? 33  LEU   A CB  1 
ATOM   293  C CG  . LEU   A 1 36  ? -13.397 -0.992  38.132  1.00 46.27  ? 33  LEU   A CG  1 
ATOM   294  C CD1 . LEU   A 1 36  ? -12.060 -1.412  37.527  1.00 42.74  ? 33  LEU   A CD1 1 
ATOM   295  C CD2 . LEU   A 1 36  ? -13.951 0.225   37.396  1.00 44.70  ? 33  LEU   A CD2 1 
ATOM   296  N N   . GLY   A 1 37  ? -17.732 -2.816  37.647  1.00 44.07  ? 34  GLY   A N   1 
ATOM   297  C CA  . GLY   A 1 37  ? -18.512 -3.898  37.083  1.00 45.26  ? 34  GLY   A CA  1 
ATOM   298  C C   . GLY   A 1 37  ? -17.650 -4.830  36.249  1.00 52.79  ? 34  GLY   A C   1 
ATOM   299  O O   . GLY   A 1 37  ? -16.487 -4.563  35.946  1.00 54.38  ? 34  GLY   A O   1 
ATOM   300  N N   . GLU   A 1 38  ? -18.257 -5.953  35.857  1.00 51.64  ? 35  GLU   A N   1 
ATOM   301  C CA  . GLU   A 1 38  ? -17.510 -7.033  35.212  1.00 54.00  ? 35  GLU   A CA  1 
ATOM   302  C C   . GLU   A 1 38  ? -16.792 -6.576  33.941  1.00 53.63  ? 35  GLU   A C   1 
ATOM   303  O O   . GLU   A 1 38  ? -15.746 -7.134  33.587  1.00 49.66  ? 35  GLU   A O   1 
ATOM   304  C CB  . GLU   A 1 38  ? -18.456 -8.203  34.895  1.00 56.63  ? 35  GLU   A CB  1 
ATOM   305  C CG  . GLU   A 1 38  ? -18.959 -9.005  36.108  1.00 56.32  ? 35  GLU   A CG  1 
ATOM   306  C CD  . GLU   A 1 38  ? -19.939 -8.236  36.994  1.00 62.26  ? 35  GLU   A CD  1 
ATOM   307  O OE1 . GLU   A 1 38  ? -20.653 -7.342  36.461  1.00 53.14  ? 35  GLU   A OE1 1 
ATOM   308  O OE2 . GLU   A 1 38  ? -19.985 -8.532  38.222  1.00 63.59  ? 35  GLU   A OE2 1 
ATOM   309  N N   . GLU   A 1 39  ? -17.326 -5.573  33.241  1.00 49.80  ? 36  GLU   A N   1 
ATOM   310  C CA  . GLU   A 1 39  ? -16.733 -5.110  31.986  1.00 53.39  ? 36  GLU   A CA  1 
ATOM   311  C C   . GLU   A 1 39  ? -16.267 -3.662  32.034  1.00 54.25  ? 36  GLU   A C   1 
ATOM   312  O O   . GLU   A 1 39  ? -15.878 -3.117  30.993  1.00 53.62  ? 36  GLU   A O   1 
ATOM   313  C CB  . GLU   A 1 39  ? -17.722 -5.260  30.832  1.00 51.11  ? 36  GLU   A CB  1 
ATOM   314  C CG  . GLU   A 1 39  ? -18.157 -6.663  30.552  1.00 55.22  ? 36  GLU   A CG  1 
ATOM   315  C CD  . GLU   A 1 39  ? -19.186 -6.704  29.448  1.00 56.36  ? 36  GLU   A CD  1 
ATOM   316  O OE1 . GLU   A 1 39  ? -20.291 -6.139  29.638  1.00 48.68  ? 36  GLU   A OE1 1 
ATOM   317  O OE2 . GLU   A 1 39  ? -18.868 -7.274  28.382  1.00 59.74  ? 36  GLU   A OE2 1 
ATOM   318  N N   . GLN   A 1 40  ? -16.311 -3.022  33.199  1.00 47.41  ? 37  GLN   A N   1 
ATOM   319  C CA  . GLN   A 1 40  ? -15.916 -1.628  33.288  1.00 45.40  ? 37  GLN   A CA  1 
ATOM   320  C C   . GLN   A 1 40  ? -14.403 -1.478  33.445  1.00 47.83  ? 37  GLN   A C   1 
ATOM   321  O O   . GLN   A 1 40  ? -13.679 -2.425  33.786  1.00 44.46  ? 37  GLN   A O   1 
ATOM   322  C CB  . GLN   A 1 40  ? -16.623 -0.950  34.447  1.00 45.04  ? 37  GLN   A CB  1 
ATOM   323  C CG  . GLN   A 1 40  ? -18.097 -0.846  34.277  1.00 46.18  ? 37  GLN   A CG  1 
ATOM   324  C CD  . GLN   A 1 40  ? -18.696 0.035   35.339  1.00 50.41  ? 37  GLN   A CD  1 
ATOM   325  O OE1 . GLN   A 1 40  ? -18.132 0.165   36.428  1.00 52.70  ? 37  GLN   A OE1 1 
ATOM   326  N NE2 . GLN   A 1 40  ? -19.830 0.668   35.032  1.00 50.18  ? 37  GLN   A NE2 1 
ATOM   327  N N   . MET   A 1 41  ? -13.935 -0.250  33.194  1.00 42.46  ? 38  MET   A N   1 
ATOM   328  C CA  . MET   A 1 41  ? -12.535 0.114   33.333  1.00 39.32  ? 38  MET   A CA  1 
ATOM   329  C C   . MET   A 1 41  ? -12.415 1.406   34.125  1.00 36.84  ? 38  MET   A C   1 
ATOM   330  O O   . MET   A 1 41  ? -13.301 2.266   34.076  1.00 35.52  ? 38  MET   A O   1 
ATOM   331  C CB  . MET   A 1 41  ? -11.880 0.279   31.976  1.00 36.29  ? 38  MET   A CB  1 
ATOM   332  C CG  . MET   A 1 41  ? -11.629 -1.021  31.255  1.00 37.73  ? 38  MET   A CG  1 
ATOM   333  S SD  . MET   A 1 41  ? -11.590 -0.788  29.466  1.00 46.68  ? 38  MET   A SD  1 
ATOM   334  C CE  . MET   A 1 41  ? -13.123 0.109   29.238  1.00 41.06  ? 38  MET   A CE  1 
ATOM   335  N N   . LEU   A 1 42  ? -11.320 1.531   34.869  1.00 33.58  ? 39  LEU   A N   1 
ATOM   336  C CA  . LEU   A 1 42  ? -10.960 2.795   35.502  1.00 34.44  ? 39  LEU   A CA  1 
ATOM   337  C C   . LEU   A 1 42  ? -9.843  3.425   34.685  1.00 34.09  ? 39  LEU   A C   1 
ATOM   338  O O   . LEU   A 1 42  ? -8.766  2.837   34.546  1.00 37.04  ? 39  LEU   A O   1 
ATOM   339  C CB  . LEU   A 1 42  ? -10.509 2.604   36.944  1.00 31.75  ? 39  LEU   A CB  1 
ATOM   340  C CG  . LEU   A 1 42  ? -10.002 3.925   37.509  1.00 36.63  ? 39  LEU   A CG  1 
ATOM   341  C CD1 . LEU   A 1 42  ? -11.170 4.920   37.712  1.00 35.03  ? 39  LEU   A CD1 1 
ATOM   342  C CD2 . LEU   A 1 42  ? -9.210  3.711   38.788  1.00 35.91  ? 39  LEU   A CD2 1 
ATOM   343  N N   . LEU   A 1 43  ? -10.093 4.614   34.152  1.00 30.35  ? 40  LEU   A N   1 
ATOM   344  C CA  . LEU   A 1 43  ? -9.222  5.207   33.153  1.00 35.16  ? 40  LEU   A CA  1 
ATOM   345  C C   . LEU   A 1 43  ? -8.638  6.520   33.656  1.00 37.79  ? 40  LEU   A C   1 
ATOM   346  O O   . LEU   A 1 43  ? -9.314  7.295   34.347  1.00 37.48  ? 40  LEU   A O   1 
ATOM   347  C CB  . LEU   A 1 43  ? -9.986  5.427   31.833  1.00 37.02  ? 40  LEU   A CB  1 
ATOM   348  C CG  . LEU   A 1 43  ? -10.633 4.154   31.274  1.00 36.81  ? 40  LEU   A CG  1 
ATOM   349  C CD1 . LEU   A 1 43  ? -12.068 4.399   30.854  1.00 36.48  ? 40  LEU   A CD1 1 
ATOM   350  C CD2 . LEU   A 1 43  ? -9.818  3.550   30.134  1.00 30.67  ? 40  LEU   A CD2 1 
ATOM   351  N N   . LYS   A 1 44  ? -7.367  6.741   33.324  1.00 33.15  ? 41  LYS   A N   1 
ATOM   352  C CA  . LYS   A 1 44  ? -6.697  8.017   33.511  1.00 35.21  ? 41  LYS   A CA  1 
ATOM   353  C C   . LYS   A 1 44  ? -6.526  8.694   32.151  1.00 39.06  ? 41  LYS   A C   1 
ATOM   354  O O   . LYS   A 1 44  ? -6.144  8.047   31.166  1.00 37.36  ? 41  LYS   A O   1 
ATOM   355  C CB  . LYS   A 1 44  ? -5.337  7.816   34.171  1.00 34.90  ? 41  LYS   A CB  1 
ATOM   356  C CG  . LYS   A 1 44  ? -4.610  9.105   34.491  1.00 35.25  ? 41  LYS   A CG  1 
ATOM   357  C CD  . LYS   A 1 44  ? -3.208  8.817   34.990  1.00 35.41  ? 41  LYS   A CD  1 
ATOM   358  C CE  . LYS   A 1 44  ? -2.683  9.962   35.839  1.00 42.79  ? 41  LYS   A CE  1 
ATOM   359  N NZ  . LYS   A 1 44  ? -1.633  10.722  35.129  1.00 47.99  ? 41  LYS   A NZ  1 
ATOM   360  N N   . THR   A 1 45  ? -6.811  9.997   32.102  1.00 33.81  ? 42  THR   A N   1 
ATOM   361  C CA  . THR   A 1 45  ? -6.735  10.779  30.876  1.00 32.61  ? 42  THR   A CA  1 
ATOM   362  C C   . THR   A 1 45  ? -5.310  11.269  30.667  1.00 34.82  ? 42  THR   A C   1 
ATOM   363  O O   . THR   A 1 45  ? -4.761  11.963  31.528  1.00 34.25  ? 42  THR   A O   1 
ATOM   364  C CB  . THR   A 1 45  ? -7.675  11.977  30.950  1.00 31.30  ? 42  THR   A CB  1 
ATOM   365  O OG1 . THR   A 1 45  ? -8.989  11.538  31.306  1.00 31.79  ? 42  THR   A OG1 1 
ATOM   366  C CG2 . THR   A 1 45  ? -7.731  12.668  29.619  1.00 33.04  ? 42  THR   A CG2 1 
ATOM   367  N N   . LEU   A 1 46  ? -4.722  10.939  29.520  1.00 35.25  ? 43  LEU   A N   1 
ATOM   368  C CA  . LEU   A 1 46  ? -3.389  11.432  29.177  1.00 32.80  ? 43  LEU   A CA  1 
ATOM   369  C C   . LEU   A 1 46  ? -3.414  12.665  28.276  1.00 34.55  ? 43  LEU   A C   1 
ATOM   370  O O   . LEU   A 1 46  ? -2.594  13.564  28.462  1.00 38.44  ? 43  LEU   A O   1 
ATOM   371  C CB  . LEU   A 1 46  ? -2.568  10.337  28.487  1.00 30.48  ? 43  LEU   A CB  1 
ATOM   372  C CG  . LEU   A 1 46  ? -2.448  8.985   29.194  1.00 37.14  ? 43  LEU   A CG  1 
ATOM   373  C CD1 . LEU   A 1 46  ? -1.567  8.073   28.398  1.00 35.64  ? 43  LEU   A CD1 1 
ATOM   374  C CD2 . LEU   A 1 46  ? -1.884  9.154   30.575  1.00 33.07  ? 43  LEU   A CD2 1 
ATOM   375  N N   . TYR   A 1 47  ? -4.306  12.712  27.281  1.00 33.71  ? 44  TYR   A N   1 
ATOM   376  C CA  . TYR   A 1 47  ? -4.432  13.828  26.344  1.00 32.34  ? 44  TYR   A CA  1 
ATOM   377  C C   . TYR   A 1 47  ? -5.911  14.082  26.066  1.00 34.40  ? 44  TYR   A C   1 
ATOM   378  O O   . TYR   A 1 47  ? -6.727  13.158  26.039  1.00 32.66  ? 44  TYR   A O   1 
ATOM   379  C CB  . TYR   A 1 47  ? -3.731  13.582  24.987  1.00 29.98  ? 44  TYR   A CB  1 
ATOM   380  C CG  . TYR   A 1 47  ? -2.250  13.250  25.024  1.00 32.45  ? 44  TYR   A CG  1 
ATOM   381  C CD1 . TYR   A 1 47  ? -1.816  11.926  25.138  1.00 29.05  ? 44  TYR   A CD1 1 
ATOM   382  C CD2 . TYR   A 1 47  ? -1.284  14.254  24.912  1.00 31.15  ? 44  TYR   A CD2 1 
ATOM   383  C CE1 . TYR   A 1 47  ? -0.459  11.614  25.189  1.00 26.63  ? 44  TYR   A CE1 1 
ATOM   384  C CE2 . TYR   A 1 47  ? 0.072   13.953  24.944  1.00 28.70  ? 44  TYR   A CE2 1 
ATOM   385  C CZ  . TYR   A 1 47  ? 0.480   12.632  25.091  1.00 31.42  ? 44  TYR   A CZ  1 
ATOM   386  O OH  . TYR   A 1 47  ? 1.832   12.327  25.132  1.00 30.85  ? 44  TYR   A OH  1 
ATOM   387  N N   . VAL   A 1 48  ? -6.245  15.341  25.826  1.00 32.59  ? 45  VAL   A N   1 
ATOM   388  C CA  . VAL   A 1 48  ? -7.615  15.756  25.553  1.00 31.48  ? 45  VAL   A CA  1 
ATOM   389  C C   . VAL   A 1 48  ? -7.605  16.634  24.307  1.00 35.69  ? 45  VAL   A C   1 
ATOM   390  O O   . VAL   A 1 48  ? -6.678  17.432  24.104  1.00 35.93  ? 45  VAL   A O   1 
ATOM   391  C CB  . VAL   A 1 48  ? -8.224  16.499  26.768  1.00 36.62  ? 45  VAL   A CB  1 
ATOM   392  C CG1 . VAL   A 1 48  ? -9.356  17.404  26.361  1.00 36.46  ? 45  VAL   A CG1 1 
ATOM   393  C CG2 . VAL   A 1 48  ? -8.714  15.512  27.798  1.00 36.65  ? 45  VAL   A CG2 1 
ATOM   394  N N   . SER   A 1 49  ? -8.617  16.456  23.456  1.00 29.35  ? 46  SER   A N   1 
ATOM   395  C CA  . SER   A 1 49  ? -8.804  17.279  22.273  1.00 33.66  ? 46  SER   A CA  1 
ATOM   396  C C   . SER   A 1 49  ? -9.692  18.482  22.584  1.00 34.78  ? 46  SER   A C   1 
ATOM   397  O O   . SER   A 1 49  ? -10.597 18.414  23.421  1.00 36.66  ? 46  SER   A O   1 
ATOM   398  C CB  . SER   A 1 49  ? -9.432  16.453  21.151  1.00 36.17  ? 46  SER   A CB  1 
ATOM   399  O OG  . SER   A 1 49  ? -9.398  17.136  19.917  1.00 35.32  ? 46  SER   A OG  1 
ATOM   400  N N   . VAL   A 1 50  ? -9.418  19.596  21.911  1.00 30.78  ? 47  VAL   A N   1 
ATOM   401  C CA  . VAL   A 1 50  ? -10.358 20.711  21.829  1.00 34.30  ? 47  VAL   A CA  1 
ATOM   402  C C   . VAL   A 1 50  ? -10.664 20.965  20.353  1.00 35.17  ? 47  VAL   A C   1 
ATOM   403  O O   . VAL   A 1 50  ? -9.750  21.029  19.518  1.00 30.31  ? 47  VAL   A O   1 
ATOM   404  C CB  . VAL   A 1 50  ? -9.823  21.978  22.528  1.00 34.42  ? 47  VAL   A CB  1 
ATOM   405  C CG1 . VAL   A 1 50  ? -9.680  21.720  24.019  1.00 36.98  ? 47  VAL   A CG1 1 
ATOM   406  C CG2 . VAL   A 1 50  ? -8.478  22.400  21.955  1.00 33.06  ? 47  VAL   A CG2 1 
ATOM   407  N N   . ASP   A 1 51  ? -11.947 21.087  20.037  1.00 30.84  ? 48  ASP   A N   1 
ATOM   408  C CA  . ASP   A 1 51  ? -12.421 21.170  18.675  1.00 36.94  ? 48  ASP   A CA  1 
ATOM   409  C C   . ASP   A 1 51  ? -13.599 22.125  18.616  1.00 44.03  ? 48  ASP   A C   1 
ATOM   410  O O   . ASP   A 1 51  ? -14.329 22.272  19.602  1.00 41.04  ? 48  ASP   A O   1 
ATOM   411  C CB  . ASP   A 1 51  ? -12.860 19.796  18.156  1.00 36.34  ? 48  ASP   A CB  1 
ATOM   412  C CG  . ASP   A 1 51  ? -11.801 18.749  18.342  1.00 40.64  ? 48  ASP   A CG  1 
ATOM   413  O OD1 . ASP   A 1 51  ? -11.598 18.314  19.508  1.00 41.64  ? 48  ASP   A OD1 1 
ATOM   414  O OD2 . ASP   A 1 51  ? -11.176 18.358  17.331  1.00 39.56  ? 48  ASP   A OD2 1 
ATOM   415  N N   . PRO   A 1 52  ? -13.820 22.774  17.467  1.00 46.56  ? 49  PRO   A N   1 
ATOM   416  C CA  . PRO   A 1 52  ? -14.987 23.667  17.350  1.00 43.98  ? 49  PRO   A CA  1 
ATOM   417  C C   . PRO   A 1 52  ? -16.328 22.981  17.567  1.00 41.53  ? 49  PRO   A C   1 
ATOM   418  O O   . PRO   A 1 52  ? -17.216 23.587  18.181  1.00 39.61  ? 49  PRO   A O   1 
ATOM   419  C CB  . PRO   A 1 52  ? -14.844 24.221  15.928  1.00 47.90  ? 49  PRO   A CB  1 
ATOM   420  C CG  . PRO   A 1 52  ? -13.356 24.250  15.706  1.00 48.37  ? 49  PRO   A CG  1 
ATOM   421  C CD  . PRO   A 1 52  ? -12.834 23.004  16.395  1.00 42.17  ? 49  PRO   A CD  1 
ATOM   422  N N   . TYR   A 1 53  ? -16.508 21.740  17.090  1.00 41.40  ? 50  TYR   A N   1 
ATOM   423  C CA  . TYR   A 1 53  ? -17.780 21.037  17.277  1.00 38.75  ? 50  TYR   A CA  1 
ATOM   424  C C   . TYR   A 1 53  ? -18.148 20.856  18.744  1.00 39.99  ? 50  TYR   A C   1 
ATOM   425  O O   . TYR   A 1 53  ? -19.267 20.416  19.031  1.00 38.72  ? 50  TYR   A O   1 
ATOM   426  C CB  . TYR   A 1 53  ? -17.774 19.656  16.589  1.00 41.00  ? 50  TYR   A CB  1 
ATOM   427  C CG  . TYR   A 1 53  ? -16.735 18.640  17.090  1.00 45.52  ? 50  TYR   A CG  1 
ATOM   428  C CD1 . TYR   A 1 53  ? -16.818 18.065  18.374  1.00 40.89  ? 50  TYR   A CD1 1 
ATOM   429  C CD2 . TYR   A 1 53  ? -15.690 18.230  16.263  1.00 39.48  ? 50  TYR   A CD2 1 
ATOM   430  C CE1 . TYR   A 1 53  ? -15.868 17.146  18.815  1.00 41.15  ? 50  TYR   A CE1 1 
ATOM   431  C CE2 . TYR   A 1 53  ? -14.743 17.305  16.695  1.00 35.86  ? 50  TYR   A CE2 1 
ATOM   432  C CZ  . TYR   A 1 53  ? -14.836 16.769  17.963  1.00 42.10  ? 50  TYR   A CZ  1 
ATOM   433  O OH  . TYR   A 1 53  ? -13.892 15.853  18.372  1.00 42.19  ? 50  TYR   A OH  1 
ATOM   434  N N   . LEU   A 1 54  ? -17.228 21.139  19.670  1.00 41.05  ? 51  LEU   A N   1 
ATOM   435  C CA  . LEU   A 1 54  ? -17.562 21.151  21.085  1.00 41.65  ? 51  LEU   A CA  1 
ATOM   436  C C   . LEU   A 1 54  ? -18.481 22.311  21.447  1.00 44.98  ? 51  LEU   A C   1 
ATOM   437  O O   . LEU   A 1 54  ? -19.199 22.223  22.450  1.00 41.54  ? 51  LEU   A O   1 
ATOM   438  C CB  . LEU   A 1 54  ? -16.287 21.215  21.916  1.00 39.03  ? 51  LEU   A CB  1 
ATOM   439  C CG  . LEU   A 1 54  ? -15.400 19.976  21.789  1.00 40.96  ? 51  LEU   A CG  1 
ATOM   440  C CD1 . LEU   A 1 54  ? -14.177 20.093  22.701  1.00 37.38  ? 51  LEU   A CD1 1 
ATOM   441  C CD2 . LEU   A 1 54  ? -16.189 18.699  22.087  1.00 39.37  ? 51  LEU   A CD2 1 
ATOM   442  N N   . GLN   A 1 55  ? -18.467 23.392  20.655  1.00 37.56  ? 52  GLN   A N   1 
ATOM   443  C CA  . GLN   A 1 55  ? -19.426 24.469  20.859  1.00 42.29  ? 52  GLN   A CA  1 
ATOM   444  C C   . GLN   A 1 55  ? -20.855 23.946  20.827  1.00 42.43  ? 52  GLN   A C   1 
ATOM   445  O O   . GLN   A 1 55  ? -21.682 24.333  21.658  1.00 44.07  ? 52  GLN   A O   1 
ATOM   446  C CB  . GLN   A 1 55  ? -19.226 25.557  19.802  1.00 49.38  ? 52  GLN   A CB  1 
ATOM   447  C CG  . GLN   A 1 55  ? -19.990 26.852  20.068  1.00 44.99  ? 52  GLN   A CG  1 
ATOM   448  C CD  . GLN   A 1 55  ? -21.367 26.890  19.427  1.00 43.44  ? 52  GLN   A CD  1 
ATOM   449  O OE1 . GLN   A 1 55  ? -21.889 25.882  18.932  1.00 41.92  ? 52  GLN   A OE1 1 
ATOM   450  N NE2 . GLN   A 1 55  ? -21.964 28.075  19.430  1.00 49.52  ? 52  GLN   A NE2 1 
ATOM   451  N N   . GLY   A 1 56  ? -21.163 23.060  19.877  1.00 40.13  ? 53  GLY   A N   1 
ATOM   452  C CA  . GLY   A 1 56  ? -22.508 22.528  19.788  1.00 42.97  ? 53  GLY   A CA  1 
ATOM   453  C C   . GLY   A 1 56  ? -22.795 21.439  20.795  1.00 47.79  ? 53  GLY   A C   1 
ATOM   454  O O   . GLY   A 1 56  ? -23.933 21.315  21.263  1.00 47.60  ? 53  GLY   A O   1 
ATOM   455  N N   . ILE   A 1 57  ? -21.785 20.622  21.119  1.00 48.17  ? 54  ILE   A N   1 
ATOM   456  C CA  . ILE   A 1 57  ? -21.931 19.582  22.139  1.00 47.19  ? 54  ILE   A CA  1 
ATOM   457  C C   . ILE   A 1 57  ? -22.252 20.216  23.483  1.00 47.57  ? 54  ILE   A C   1 
ATOM   458  O O   . ILE   A 1 57  ? -23.181 19.802  24.186  1.00 48.94  ? 54  ILE   A O   1 
ATOM   459  C CB  . ILE   A 1 57  ? -20.646 18.737  22.230  1.00 49.41  ? 54  ILE   A CB  1 
ATOM   460  C CG1 . ILE   A 1 57  ? -20.279 18.139  20.866  1.00 46.18  ? 54  ILE   A CG1 1 
ATOM   461  C CG2 . ILE   A 1 57  ? -20.771 17.677  23.317  1.00 46.92  ? 54  ILE   A CG2 1 
ATOM   462  C CD1 . ILE   A 1 57  ? -20.917 16.826  20.576  1.00 44.59  ? 54  ILE   A CD1 1 
ATOM   463  N N   . CYS   A 1 58  ? -21.485 21.247  23.843  1.00 46.20  ? 55  CYS   A N   1 
ATOM   464  C CA  . CYS   A 1 58  ? -21.667 21.965  25.096  1.00 46.75  ? 55  CYS   A CA  1 
ATOM   465  C C   . CYS   A 1 58  ? -23.108 22.425  25.282  1.00 46.90  ? 55  CYS   A C   1 
ATOM   466  O O   . CYS   A 1 58  ? -23.730 22.139  26.307  1.00 52.65  ? 55  CYS   A O   1 
ATOM   467  C CB  . CYS   A 1 58  ? -20.712 23.154  25.125  1.00 49.37  ? 55  CYS   A CB  1 
ATOM   468  S SG  . CYS   A 1 58  ? -20.605 23.952  26.700  1.00 44.92  ? 55  CYS   A SG  1 
ATOM   469  N N   . LEU   A 1 59  ? -23.657 23.135  24.292  1.00 52.48  ? 56  LEU   A N   1 
ATOM   470  C CA  . LEU   A 1 59  ? -25.030 23.634  24.367  1.00 51.83  ? 56  LEU   A CA  1 
ATOM   471  C C   . LEU   A 1 59  ? -26.054 22.521  24.552  1.00 48.89  ? 56  LEU   A C   1 
ATOM   472  O O   . LEU   A 1 59  ? -27.193 22.804  24.938  1.00 55.52  ? 56  LEU   A O   1 
ATOM   473  C CB  . LEU   A 1 59  ? -25.362 24.451  23.113  1.00 46.97  ? 56  LEU   A CB  1 
ATOM   474  C CG  . LEU   A 1 59  ? -24.543 25.738  22.947  1.00 47.98  ? 56  LEU   A CG  1 
ATOM   475  C CD1 . LEU   A 1 59  ? -24.739 26.367  21.579  1.00 42.51  ? 56  LEU   A CD1 1 
ATOM   476  C CD2 . LEU   A 1 59  ? -24.900 26.736  24.035  1.00 49.89  ? 56  LEU   A CD2 1 
ATOM   477  N N   . ASP   A 1 60  ? -25.675 21.270  24.308  1.00 47.11  ? 57  ASP   A N   1 
ATOM   478  C CA  . ASP   A 1 60  ? -26.547 20.122  24.507  1.00 50.16  ? 57  ASP   A CA  1 
ATOM   479  C C   . ASP   A 1 60  ? -26.189 19.344  25.766  1.00 50.39  ? 57  ASP   A C   1 
ATOM   480  O O   . ASP   A 1 60  ? -26.770 18.283  26.022  1.00 46.25  ? 57  ASP   A O   1 
ATOM   481  C CB  . ASP   A 1 60  ? -26.499 19.198  23.286  1.00 51.99  ? 57  ASP   A CB  1 
ATOM   482  C CG  . ASP   A 1 60  ? -27.245 19.772  22.079  1.00 57.65  ? 57  ASP   A CG  1 
ATOM   483  O OD1 . ASP   A 1 60  ? -27.905 20.828  22.207  1.00 59.76  ? 57  ASP   A OD1 1 
ATOM   484  O OD2 . ASP   A 1 60  ? -27.171 19.158  20.996  1.00 59.25  ? 57  ASP   A OD2 1 
ATOM   485  N N   . THR   A 1 61  ? -25.239 19.847  26.546  1.00 46.23  ? 58  THR   A N   1 
ATOM   486  C CA  . THR   A 1 61  ? -24.812 19.179  27.763  1.00 50.43  ? 58  THR   A CA  1 
ATOM   487  C C   . THR   A 1 61  ? -25.614 19.713  28.939  1.00 54.14  ? 58  THR   A C   1 
ATOM   488  O O   . THR   A 1 61  ? -25.567 20.923  29.202  1.00 53.13  ? 58  THR   A O   1 
ATOM   489  C CB  . THR   A 1 61  ? -23.335 19.412  28.012  1.00 52.02  ? 58  THR   A CB  1 
ATOM   490  O OG1 . THR   A 1 61  ? -22.573 18.895  26.910  1.00 47.61  ? 58  THR   A OG1 1 
ATOM   491  C CG2 . THR   A 1 61  ? -22.910 18.747  29.324  1.00 42.77  ? 58  THR   A CG2 1 
ATOM   492  N N   . PRO   A 1 62  ? -26.368 18.873  29.647  1.00 54.57  ? 59  PRO   A N   1 
ATOM   493  C CA  . PRO   A 1 62  ? -27.035 19.328  30.873  1.00 52.63  ? 59  PRO   A CA  1 
ATOM   494  C C   . PRO   A 1 62  ? -26.076 20.092  31.771  1.00 50.68  ? 59  PRO   A C   1 
ATOM   495  O O   . PRO   A 1 62  ? -24.933 19.677  31.981  1.00 52.32  ? 59  PRO   A O   1 
ATOM   496  C CB  . PRO   A 1 62  ? -27.502 18.024  31.523  1.00 43.90  ? 59  PRO   A CB  1 
ATOM   497  C CG  . PRO   A 1 62  ? -27.719 17.099  30.362  1.00 52.03  ? 59  PRO   A CG  1 
ATOM   498  C CD  . PRO   A 1 62  ? -26.666 17.462  29.338  1.00 52.11  ? 59  PRO   A CD  1 
ATOM   499  N N   . ILE   A 1 63  ? -26.539 21.251  32.251  1.00 51.78  ? 60  ILE   A N   1 
ATOM   500  C CA  . ILE   A 1 63  ? -25.764 22.062  33.182  1.00 54.06  ? 60  ILE   A CA  1 
ATOM   501  C C   . ILE   A 1 63  ? -25.293 21.205  34.354  1.00 51.54  ? 60  ILE   A C   1 
ATOM   502  O O   . ILE   A 1 63  ? -26.032 20.363  34.877  1.00 50.13  ? 60  ILE   A O   1 
ATOM   503  C CB  . ILE   A 1 63  ? -26.616 23.259  33.645  1.00 54.54  ? 60  ILE   A CB  1 
ATOM   504  C CG1 . ILE   A 1 63  ? -27.099 24.047  32.423  1.00 52.52  ? 60  ILE   A CG1 1 
ATOM   505  C CG2 . ILE   A 1 63  ? -25.837 24.162  34.599  1.00 50.88  ? 60  ILE   A CG2 1 
ATOM   506  C CD1 . ILE   A 1 63  ? -25.988 24.797  31.687  1.00 53.44  ? 60  ILE   A CD1 1 
ATOM   507  N N   . GLY   A 1 64  ? -24.040 21.398  34.751  1.00 52.13  ? 61  GLY   A N   1 
ATOM   508  C CA  . GLY   A 1 64  ? -23.438 20.611  35.797  1.00 54.71  ? 61  GLY   A CA  1 
ATOM   509  C C   . GLY   A 1 64  ? -22.699 19.375  35.319  1.00 55.48  ? 61  GLY   A C   1 
ATOM   510  O O   . GLY   A 1 64  ? -21.749 18.947  35.983  1.00 56.95  ? 61  GLY   A O   1 
ATOM   511  N N   . ASP   A 1 65  ? -23.107 18.787  34.192  1.00 50.71  ? 62  ASP   A N   1 
ATOM   512  C CA  . ASP   A 1 65  ? -22.403 17.631  33.651  1.00 47.41  ? 62  ASP   A CA  1 
ATOM   513  C C   . ASP   A 1 65  ? -21.028 18.028  33.117  1.00 49.19  ? 62  ASP   A C   1 
ATOM   514  O O   . ASP   A 1 65  ? -20.706 19.208  32.948  1.00 49.81  ? 62  ASP   A O   1 
ATOM   515  C CB  . ASP   A 1 65  ? -23.216 16.968  32.551  1.00 43.51  ? 62  ASP   A CB  1 
ATOM   516  C CG  . ASP   A 1 65  ? -24.505 16.414  33.065  1.00 52.09  ? 62  ASP   A CG  1 
ATOM   517  O OD1 . ASP   A 1 65  ? -24.807 16.650  34.259  1.00 58.50  ? 62  ASP   A OD1 1 
ATOM   518  O OD2 . ASP   A 1 65  ? -25.211 15.737  32.293  1.00 56.23  ? 62  ASP   A OD2 1 
ATOM   519  N N   . HIS   A 1 66  ? -20.200 17.016  32.869  1.00 46.72  ? 63  HIS   A N   1 
ATOM   520  C CA  . HIS   A 1 66  ? -18.842 17.274  32.421  1.00 44.42  ? 63  HIS   A CA  1 
ATOM   521  C C   . HIS   A 1 66  ? -18.840 17.568  30.927  1.00 41.99  ? 63  HIS   A C   1 
ATOM   522  O O   . HIS   A 1 66  ? -19.719 17.118  30.183  1.00 38.85  ? 63  HIS   A O   1 
ATOM   523  C CB  . HIS   A 1 66  ? -17.925 16.084  32.735  1.00 39.17  ? 63  HIS   A CB  1 
ATOM   524  C CG  . HIS   A 1 66  ? -18.169 14.875  31.880  1.00 43.30  ? 63  HIS   A CG  1 
ATOM   525  N ND1 . HIS   A 1 66  ? -17.480 14.637  30.705  1.00 39.60  ? 63  HIS   A ND1 1 
ATOM   526  C CD2 . HIS   A 1 66  ? -19.022 13.833  32.033  1.00 40.46  ? 63  HIS   A CD2 1 
ATOM   527  C CE1 . HIS   A 1 66  ? -17.901 13.504  30.171  1.00 37.09  ? 63  HIS   A CE1 1 
ATOM   528  N NE2 . HIS   A 1 66  ? -18.836 12.997  30.956  1.00 41.31  ? 63  HIS   A NE2 1 
ATOM   529  N N   . MET   A 1 67  ? -17.844 18.339  30.493  1.00 38.99  ? 64  MET   A N   1 
ATOM   530  C CA  . MET   A 1 67  ? -17.686 18.628  29.073  1.00 42.82  ? 64  MET   A CA  1 
ATOM   531  C C   . MET   A 1 67  ? -17.137 17.398  28.350  1.00 42.25  ? 64  MET   A C   1 
ATOM   532  O O   . MET   A 1 67  ? -16.020 16.944  28.639  1.00 36.75  ? 64  MET   A O   1 
ATOM   533  C CB  . MET   A 1 67  ? -16.770 19.832  28.859  1.00 39.18  ? 64  MET   A CB  1 
ATOM   534  C CG  . MET   A 1 67  ? -16.747 20.297  27.401  1.00 42.55  ? 64  MET   A CG  1 
ATOM   535  S SD  . MET   A 1 67  ? -18.413 20.635  26.762  1.00 46.44  ? 64  MET   A SD  1 
ATOM   536  C CE  . MET   A 1 67  ? -18.316 19.972  25.098  1.00 47.83  ? 64  MET   A CE  1 
ATOM   537  N N   . GLY   A 1 68  ? -17.931 16.860  27.416  1.00 35.59  ? 65  GLY   A N   1 
ATOM   538  C CA  . GLY   A 1 68  ? -17.474 15.751  26.611  1.00 36.29  ? 65  GLY   A CA  1 
ATOM   539  C C   . GLY   A 1 68  ? -16.425 16.180  25.601  1.00 43.27  ? 65  GLY   A C   1 
ATOM   540  O O   . GLY   A 1 68  ? -16.338 17.353  25.205  1.00 41.31  ? 65  GLY   A O   1 
ATOM   541  N N   . ALA   A 1 69  ? -15.593 15.207  25.201  1.00 35.54  ? 66  ALA   A N   1 
ATOM   542  C CA  . ALA   A 1 69  ? -14.491 15.454  24.275  1.00 37.97  ? 66  ALA   A CA  1 
ATOM   543  C C   . ALA   A 1 69  ? -13.724 14.185  23.940  1.00 38.61  ? 66  ALA   A C   1 
ATOM   544  O O   . ALA   A 1 69  ? -13.716 13.223  24.715  1.00 33.68  ? 66  ALA   A O   1 
ATOM   545  C CB  . ALA   A 1 69  ? -13.503 16.475  24.834  1.00 34.62  ? 66  ALA   A CB  1 
ATOM   546  N N   . ASP   A 1 70  ? -13.097 14.189  22.766  1.00 36.94  ? 67  ASP   A N   1 
ATOM   547  C CA  . ASP   A 1 70  ? -12.180 13.130  22.372  1.00 35.37  ? 67  ASP   A CA  1 
ATOM   548  C C   . ASP   A 1 70  ? -10.932 13.147  23.256  1.00 31.29  ? 67  ASP   A C   1 
ATOM   549  O O   . ASP   A 1 70  ? -10.396 14.211  23.573  1.00 32.17  ? 67  ASP   A O   1 
ATOM   550  C CB  . ASP   A 1 70  ? -11.790 13.323  20.906  1.00 33.37  ? 67  ASP   A CB  1 
ATOM   551  C CG  . ASP   A 1 70  ? -11.485 12.020  20.211  1.00 43.54  ? 67  ASP   A CG  1 
ATOM   552  O OD1 . ASP   A 1 70  ? -11.582 10.960  20.891  1.00 34.83  ? 67  ASP   A OD1 1 
ATOM   553  O OD2 . ASP   A 1 70  ? -11.151 12.064  18.986  1.00 46.96  ? 67  ASP   A OD2 1 
ATOM   554  N N   . SER   A 1 71  ? -10.445 11.969  23.632  1.00 24.76  ? 68  SER   A N   1 
ATOM   555  C CA  . SER   A 1 71  ? -9.308  11.933  24.537  1.00 31.29  ? 68  SER   A CA  1 
ATOM   556  C C   . SER   A 1 71  ? -8.563  10.610  24.415  1.00 29.38  ? 68  SER   A C   1 
ATOM   557  O O   . SER   A 1 71  ? -9.061  9.639   23.845  1.00 30.19  ? 68  SER   A O   1 
ATOM   558  C CB  . SER   A 1 71  ? -9.750  12.133  25.982  1.00 29.67  ? 68  SER   A CB  1 
ATOM   559  O OG  . SER   A 1 71  ? -10.438 10.977  26.439  1.00 34.34  ? 68  SER   A OG  1 
ATOM   560  N N   . ILE   A 1 72  ? -7.364  10.583  24.996  1.00 26.31  ? 69  ILE   A N   1 
ATOM   561  C CA  . ILE   A 1 72  ? -6.543  9.385   25.099  1.00 26.60  ? 69  ILE   A CA  1 
ATOM   562  C C   . ILE   A 1 72  ? -6.452  9.010   26.573  1.00 31.61  ? 69  ILE   A C   1 
ATOM   563  O O   . ILE   A 1 72  ? -6.100  9.847   27.418  1.00 32.34  ? 69  ILE   A O   1 
ATOM   564  C CB  . ILE   A 1 72  ? -5.144  9.600   24.489  1.00 31.52  ? 69  ILE   A CB  1 
ATOM   565  C CG1 . ILE   A 1 72  ? -5.250  9.881   22.971  1.00 29.94  ? 69  ILE   A CG1 1 
ATOM   566  C CG2 . ILE   A 1 72  ? -4.221  8.402   24.806  1.00 21.85  ? 69  ILE   A CG2 1 
ATOM   567  C CD1 . ILE   A 1 72  ? -3.944  10.339  22.311  1.00 23.02  ? 69  ILE   A CD1 1 
ATOM   568  N N   . MET   A 1 73  ? -6.772  7.757   26.882  1.00 29.01  ? 70  MET   A N   1 
ATOM   569  C CA  . MET   A 1 73  ? -6.858  7.290   28.252  1.00 32.35  ? 70  MET   A CA  1 
ATOM   570  C C   . MET   A 1 73  ? -5.987  6.058   28.446  1.00 32.79  ? 70  MET   A C   1 
ATOM   571  O O   . MET   A 1 73  ? -5.729  5.313   27.496  1.00 29.87  ? 70  MET   A O   1 
ATOM   572  C CB  . MET   A 1 73  ? -8.304  6.979   28.607  1.00 31.64  ? 70  MET   A CB  1 
ATOM   573  C CG  . MET   A 1 73  ? -9.202  8.186   28.490  1.00 31.68  ? 70  MET   A CG  1 
ATOM   574  S SD  . MET   A 1 73  ? -10.948 7.730   28.426  1.00 39.84  ? 70  MET   A SD  1 
ATOM   575  C CE  . MET   A 1 73  ? -11.170 7.250   26.698  1.00 33.21  ? 70  MET   A CE  1 
ATOM   576  N N   . GLN   A 1 74  ? -5.529  5.856   29.686  1.00 30.82  ? 71  GLN   A N   1 
ATOM   577  C CA  . GLN   A 1 74  ? -4.858  4.624   30.083  1.00 32.36  ? 71  GLN   A CA  1 
ATOM   578  C C   . GLN   A 1 74  ? -5.686  3.877   31.124  1.00 35.95  ? 71  GLN   A C   1 
ATOM   579  O O   . GLN   A 1 74  ? -6.239  4.483   32.052  1.00 31.38  ? 71  GLN   A O   1 
ATOM   580  C CB  . GLN   A 1 74  ? -3.456  4.890   30.643  1.00 31.63  ? 71  GLN   A CB  1 
ATOM   581  C CG  . GLN   A 1 74  ? -2.629  3.620   30.744  1.00 31.86  ? 71  GLN   A CG  1 
ATOM   582  C CD  . GLN   A 1 74  ? -1.148  3.897   30.847  1.00 38.91  ? 71  GLN   A CD  1 
ATOM   583  O OE1 . GLN   A 1 74  ? -0.738  4.953   31.350  1.00 35.00  ? 71  GLN   A OE1 1 
ATOM   584  N NE2 . GLN   A 1 74  ? -0.326  2.949   30.365  1.00 39.71  ? 71  GLN   A NE2 1 
ATOM   585  N N   . VAL   A 1 75  ? -5.767  2.557   30.963  1.00 34.79  ? 72  VAL   A N   1 
ATOM   586  C CA  . VAL   A 1 75  ? -6.511  1.724   31.899  1.00 35.83  ? 72  VAL   A CA  1 
ATOM   587  C C   . VAL   A 1 75  ? -5.675  1.529   33.160  1.00 38.92  ? 72  VAL   A C   1 
ATOM   588  O O   . VAL   A 1 75  ? -4.559  0.995   33.111  1.00 33.66  ? 72  VAL   A O   1 
ATOM   589  C CB  . VAL   A 1 75  ? -6.889  0.375   31.275  1.00 40.41  ? 72  VAL   A CB  1 
ATOM   590  C CG1 . VAL   A 1 75  ? -7.628  -0.494  32.300  1.00 38.73  ? 72  VAL   A CG1 1 
ATOM   591  C CG2 . VAL   A 1 75  ? -7.735  0.579   30.030  1.00 33.94  ? 72  VAL   A CG2 1 
ATOM   592  N N   . LEU   A 1 76  ? -6.212  1.982   34.293  1.00 37.98  ? 73  LEU   A N   1 
ATOM   593  C CA  . LEU   A 1 76  ? -5.576  1.746   35.579  1.00 37.17  ? 73  LEU   A CA  1 
ATOM   594  C C   . LEU   A 1 76  ? -6.033  0.425   36.167  1.00 38.09  ? 73  LEU   A C   1 
ATOM   595  O O   . LEU   A 1 76  ? -5.237  -0.308  36.757  1.00 45.15  ? 73  LEU   A O   1 
ATOM   596  C CB  . LEU   A 1 76  ? -5.892  2.893   36.543  1.00 37.05  ? 73  LEU   A CB  1 
ATOM   597  C CG  . LEU   A 1 76  ? -5.585  4.307   36.048  1.00 36.64  ? 73  LEU   A CG  1 
ATOM   598  C CD1 . LEU   A 1 76  ? -6.282  5.314   36.926  1.00 36.78  ? 73  LEU   A CD1 1 
ATOM   599  C CD2 . LEU   A 1 76  ? -4.078  4.595   35.984  1.00 30.67  ? 73  LEU   A CD2 1 
ATOM   600  N N   . ASP   A 1 77  ? -7.297  0.090   35.962  1.00 36.00  ? 74  ASP   A N   1 
ATOM   601  C CA  . ASP   A 1 77  ? -7.886  -1.097  36.548  1.00 39.87  ? 74  ASP   A CA  1 
ATOM   602  C C   . ASP   A 1 77  ? -9.082  -1.485  35.692  1.00 39.83  ? 74  ASP   A C   1 
ATOM   603  O O   . ASP   A 1 77  ? -9.661  -0.646  34.991  1.00 41.50  ? 74  ASP   A O   1 
ATOM   604  C CB  . ASP   A 1 77  ? -8.283  -0.831  38.009  1.00 41.81  ? 74  ASP   A CB  1 
ATOM   605  C CG  . ASP   A 1 77  ? -8.592  -2.096  38.778  1.00 43.47  ? 74  ASP   A CG  1 
ATOM   606  O OD1 . ASP   A 1 77  ? -8.175  -3.198  38.335  1.00 40.71  ? 74  ASP   A OD1 1 
ATOM   607  O OD2 . ASP   A 1 77  ? -9.275  -1.983  39.823  1.00 48.83  ? 74  ASP   A OD2 1 
ATOM   608  N N   . ALA   A 1 78  ? -9.454  -2.763  35.764  1.00 42.92  ? 75  ALA   A N   1 
ATOM   609  C CA  . ALA   A 1 78  ? -10.458 -3.312  34.858  1.00 49.34  ? 75  ALA   A CA  1 
ATOM   610  C C   . ALA   A 1 78  ? -11.115 -4.546  35.466  1.00 49.73  ? 75  ALA   A C   1 
ATOM   611  O O   . ALA   A 1 78  ? -10.427 -5.441  35.963  1.00 47.82  ? 75  ALA   A O   1 
ATOM   612  C CB  . ALA   A 1 78  ? -9.832  -3.680  33.509  1.00 44.74  ? 75  ALA   A CB  1 
ATOM   613  N N   . GLY   A 1 79  ? -12.442 -4.604  35.374  1.00 51.01  ? 76  GLY   A N   1 
ATOM   614  C CA  . GLY   A 1 79  ? -13.194 -5.782  35.738  1.00 45.43  ? 76  GLY   A CA  1 
ATOM   615  C C   . GLY   A 1 79  ? -12.852 -6.979  34.873  1.00 50.43  ? 76  GLY   A C   1 
ATOM   616  O O   . GLY   A 1 79  ? -12.163 -6.873  33.854  1.00 50.09  ? 76  GLY   A O   1 
ATOM   617  N N   . PRO   A 1 80  ? -13.344 -8.153  35.267  1.00 56.46  ? 77  PRO   A N   1 
ATOM   618  C CA  . PRO   A 1 80  ? -12.856 -9.393  34.638  1.00 52.01  ? 77  PRO   A CA  1 
ATOM   619  C C   . PRO   A 1 80  ? -13.129 -9.493  33.145  1.00 55.87  ? 77  PRO   A C   1 
ATOM   620  O O   . PRO   A 1 80  ? -12.318 -10.093 32.426  1.00 56.05  ? 77  PRO   A O   1 
ATOM   621  C CB  . PRO   A 1 80  ? -13.573 -10.498 35.426  1.00 45.88  ? 77  PRO   A CB  1 
ATOM   622  C CG  . PRO   A 1 80  ? -14.627 -9.803  36.240  1.00 55.28  ? 77  PRO   A CG  1 
ATOM   623  C CD  . PRO   A 1 80  ? -14.172 -8.410  36.456  1.00 53.65  ? 77  PRO   A CD  1 
ATOM   624  N N   . ASN   A 1 81  ? -14.234 -8.940  32.646  1.00 53.78  ? 78  ASN   A N   1 
ATOM   625  C CA  . ASN   A 1 81  ? -14.560 -9.039  31.225  1.00 50.87  ? 78  ASN   A CA  1 
ATOM   626  C C   . ASN   A 1 81  ? -14.459 -7.685  30.527  1.00 53.87  ? 78  ASN   A C   1 
ATOM   627  O O   . ASN   A 1 81  ? -15.185 -7.413  29.563  1.00 49.62  ? 78  ASN   A O   1 
ATOM   628  C CB  . ASN   A 1 81  ? -15.950 -9.643  31.025  1.00 53.88  ? 78  ASN   A CB  1 
ATOM   629  C CG  . ASN   A 1 81  ? -16.130 -10.936 31.791  1.00 58.66  ? 78  ASN   A CG  1 
ATOM   630  O OD1 . ASN   A 1 81  ? -16.922 -11.001 32.738  1.00 59.27  ? 78  ASN   A OD1 1 
ATOM   631  N ND2 . ASN   A 1 81  ? -15.380 -11.970 31.400  1.00 53.33  ? 78  ASN   A ND2 1 
ATOM   632  N N   . ALA   A 1 82  ? -13.574 -6.821  31.026  1.00 55.97  ? 79  ALA   A N   1 
ATOM   633  C CA  . ALA   A 1 82  ? -13.327 -5.549  30.374  1.00 49.76  ? 79  ALA   A CA  1 
ATOM   634  C C   . ALA   A 1 82  ? -12.654 -5.793  29.030  1.00 46.46  ? 79  ALA   A C   1 
ATOM   635  O O   . ALA   A 1 82  ? -11.847 -6.720  28.895  1.00 45.56  ? 79  ALA   A O   1 
ATOM   636  C CB  . ALA   A 1 82  ? -12.445 -4.660  31.240  1.00 44.28  ? 79  ALA   A CB  1 
ATOM   637  N N   . PRO   A 1 83  ? -12.964 -4.987  28.017  1.00 41.88  ? 80  PRO   A N   1 
ATOM   638  C CA  . PRO   A 1 83  ? -12.345 -5.214  26.704  1.00 42.47  ? 80  PRO   A CA  1 
ATOM   639  C C   . PRO   A 1 83  ? -10.850 -4.956  26.695  1.00 40.05  ? 80  PRO   A C   1 
ATOM   640  O O   . PRO   A 1 83  ? -10.156 -5.514  25.840  1.00 41.60  ? 80  PRO   A O   1 
ATOM   641  C CB  . PRO   A 1 83  ? -13.104 -4.251  25.783  1.00 34.63  ? 80  PRO   A CB  1 
ATOM   642  C CG  . PRO   A 1 83  ? -13.643 -3.186  26.715  1.00 42.42  ? 80  PRO   A CG  1 
ATOM   643  C CD  . PRO   A 1 83  ? -13.875 -3.829  28.035  1.00 39.79  ? 80  PRO   A CD  1 
ATOM   644  N N   . PHE   A 1 84  ? -10.320 -4.165  27.628  1.00 39.19  ? 81  PHE   A N   1 
ATOM   645  C CA  . PHE   A 1 84  ? -8.892  -3.875  27.663  1.00 44.72  ? 81  PHE   A CA  1 
ATOM   646  C C   . PHE   A 1 84  ? -8.348  -4.103  29.074  1.00 46.76  ? 81  PHE   A C   1 
ATOM   647  O O   . PHE   A 1 84  ? -9.102  -4.136  30.050  1.00 44.78  ? 81  PHE   A O   1 
ATOM   648  C CB  . PHE   A 1 84  ? -8.631  -2.445  27.158  1.00 40.76  ? 81  PHE   A CB  1 
ATOM   649  C CG  . PHE   A 1 84  ? -9.361  -2.122  25.863  1.00 41.24  ? 81  PHE   A CG  1 
ATOM   650  C CD1 . PHE   A 1 84  ? -9.001  -2.741  24.661  1.00 39.43  ? 81  PHE   A CD1 1 
ATOM   651  C CD2 . PHE   A 1 84  ? -10.429 -1.232  25.850  1.00 38.08  ? 81  PHE   A CD2 1 
ATOM   652  C CE1 . PHE   A 1 84  ? -9.688  -2.475  23.474  1.00 32.45  ? 81  PHE   A CE1 1 
ATOM   653  C CE2 . PHE   A 1 84  ? -11.109 -0.951  24.655  1.00 38.48  ? 81  PHE   A CE2 1 
ATOM   654  C CZ  . PHE   A 1 84  ? -10.730 -1.575  23.472  1.00 33.98  ? 81  PHE   A CZ  1 
ATOM   655  N N   . ARG   A 1 85  ? -7.004  -4.299  29.172  1.00 41.11  ? 82  ARG   A N   1 
ATOM   656  C CA  . ARG   A 1 85  ? -6.333  -4.617  30.428  1.00 42.44  ? 82  ARG   A CA  1 
ATOM   657  C C   . ARG   A 1 85  ? -5.589  -3.407  30.975  1.00 43.84  ? 82  ARG   A C   1 
ATOM   658  O O   . ARG   A 1 85  ? -5.338  -2.441  30.252  1.00 42.98  ? 82  ARG   A O   1 
ATOM   659  C CB  . ARG   A 1 85  ? -5.351  -5.777  30.236  1.00 44.99  ? 82  ARG   A CB  1 
ATOM   660  C CG  . ARG   A 1 85  ? -5.985  -7.096  29.734  1.00 58.76  ? 82  ARG   A CG  1 
ATOM   661  C CD  . ARG   A 1 85  ? -7.368  -7.411  30.371  1.00 64.64  ? 82  ARG   A CD  1 
ATOM   662  N NE  . ARG   A 1 85  ? -7.349  -7.417  31.835  1.00 63.42  ? 82  ARG   A NE  1 
ATOM   663  C CZ  . ARG   A 1 85  ? -8.414  -7.608  32.605  1.00 58.17  ? 82  ARG   A CZ  1 
ATOM   664  N NH1 . ARG   A 1 85  ? -9.608  -7.861  32.089  1.00 55.63  ? 82  ARG   A NH1 1 
ATOM   665  N NH2 . ARG   A 1 85  ? -8.278  -7.529  33.927  1.00 55.49  ? 82  ARG   A NH2 1 
ATOM   666  N N   . PRO   A 1 86  ? -5.245  -3.408  32.263  1.00 46.02  ? 83  PRO   A N   1 
ATOM   667  C CA  . PRO   A 1 86  ? -4.449  -2.300  32.807  1.00 41.86  ? 83  PRO   A CA  1 
ATOM   668  C C   . PRO   A 1 86  ? -3.179  -2.081  32.001  1.00 40.52  ? 83  PRO   A C   1 
ATOM   669  O O   . PRO   A 1 86  ? -2.516  -3.028  31.579  1.00 40.64  ? 83  PRO   A O   1 
ATOM   670  C CB  . PRO   A 1 86  ? -4.140  -2.751  34.238  1.00 37.75  ? 83  PRO   A CB  1 
ATOM   671  C CG  . PRO   A 1 86  ? -5.295  -3.612  34.586  1.00 42.03  ? 83  PRO   A CG  1 
ATOM   672  C CD  . PRO   A 1 86  ? -5.761  -4.286  33.330  1.00 45.16  ? 83  PRO   A CD  1 
ATOM   673  N N   . GLY   A 1 87  ? -2.848  -0.809  31.789  1.00 41.96  ? 84  GLY   A N   1 
ATOM   674  C CA  . GLY   A 1 87  ? -1.790  -0.412  30.903  1.00 39.34  ? 84  GLY   A CA  1 
ATOM   675  C C   . GLY   A 1 87  ? -2.236  -0.137  29.480  1.00 36.79  ? 84  GLY   A C   1 
ATOM   676  O O   . GLY   A 1 87  ? -1.580  0.638   28.775  1.00 42.10  ? 84  GLY   A O   1 
ATOM   677  N N   . ASP   A 1 88  ? -3.341  -0.733  29.040  1.00 37.99  ? 85  ASP   A N   1 
ATOM   678  C CA  . ASP   A 1 88  ? -3.805  -0.502  27.672  1.00 38.99  ? 85  ASP   A CA  1 
ATOM   679  C C   . ASP   A 1 88  ? -4.186  0.961   27.468  1.00 37.40  ? 85  ASP   A C   1 
ATOM   680  O O   . ASP   A 1 88  ? -4.791  1.597   28.342  1.00 32.57  ? 85  ASP   A O   1 
ATOM   681  C CB  . ASP   A 1 88  ? -5.003  -1.399  27.331  1.00 34.50  ? 85  ASP   A CB  1 
ATOM   682  C CG  . ASP   A 1 88  ? -4.600  -2.846  27.049  1.00 40.90  ? 85  ASP   A CG  1 
ATOM   683  O OD1 . ASP   A 1 88  ? -3.386  -3.123  26.880  1.00 40.34  ? 85  ASP   A OD1 1 
ATOM   684  O OD2 . ASP   A 1 88  ? -5.509  -3.708  26.990  1.00 46.55  ? 85  ASP   A OD2 1 
ATOM   685  N N   . LEU   A 1 89  ? -3.804  1.494   26.306  1.00 34.43  ? 86  LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 89  ? -4.210  2.817   25.871  1.00 28.61  ? 86  LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 89  ? -5.435  2.715   24.969  1.00 30.90  ? 86  LEU   A C   1 
ATOM   688  O O   . LEU   A 1 89  ? -5.510  1.848   24.091  1.00 29.51  ? 86  LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 89  ? -3.063  3.499   25.134  1.00 33.25  ? 86  LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 89  ? -1.802  3.569   25.985  1.00 35.67  ? 86  LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 89  ? -0.546  3.511   25.112  1.00 34.01  ? 86  LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 89  ? -1.837  4.829   26.852  1.00 34.13  ? 86  LEU   A CD2 1 
ATOM   693  N N   . VAL   A 1 90  ? -6.397  3.605   25.185  1.00 33.08  ? 87  VAL   A N   1 
ATOM   694  C CA  . VAL   A 1 90  ? -7.587  3.664   24.352  1.00 31.24  ? 87  VAL   A CA  1 
ATOM   695  C C   . VAL   A 1 90  ? -7.842  5.105   23.947  1.00 32.58  ? 87  VAL   A C   1 
ATOM   696  O O   . VAL   A 1 90  ? -7.460  6.043   24.653  1.00 29.37  ? 87  VAL   A O   1 
ATOM   697  C CB  . VAL   A 1 90  ? -8.832  3.083   25.056  1.00 28.73  ? 87  VAL   A CB  1 
ATOM   698  C CG1 . VAL   A 1 90  ? -8.668  1.591   25.248  1.00 30.54  ? 87  VAL   A CG1 1 
ATOM   699  C CG2 . VAL   A 1 90  ? -9.065  3.795   26.378  1.00 30.11  ? 87  VAL   A CG2 1 
ATOM   700  N N   . GLN   A 1 91  ? -8.503  5.270   22.797  1.00 30.86  ? 88  GLN   A N   1 
ATOM   701  C CA  . GLN   A 1 91  ? -9.043  6.554   22.379  1.00 29.88  ? 88  GLN   A CA  1 
ATOM   702  C C   . GLN   A 1 91  ? -10.571 6.479   22.376  1.00 32.54  ? 88  GLN   A C   1 
ATOM   703  O O   . GLN   A 1 91  ? -11.156 5.480   21.937  1.00 33.12  ? 88  GLN   A O   1 
ATOM   704  C CB  . GLN   A 1 91  ? -8.494  6.940   21.000  1.00 31.96  ? 88  GLN   A CB  1 
ATOM   705  C CG  . GLN   A 1 91  ? -9.033  8.257   20.408  1.00 30.73  ? 88  GLN   A CG  1 
ATOM   706  C CD  . GLN   A 1 91  ? -10.314 8.060   19.629  1.00 30.96  ? 88  GLN   A CD  1 
ATOM   707  O OE1 . GLN   A 1 91  ? -10.418 7.181   18.770  1.00 38.77  ? 88  GLN   A OE1 1 
ATOM   708  N NE2 . GLN   A 1 91  ? -11.303 8.854   19.943  1.00 33.93  ? 88  GLN   A NE2 1 
ATOM   709  N N   . GLY   A 1 92  ? -11.207 7.534   22.876  1.00 30.86  ? 89  GLY   A N   1 
ATOM   710  C CA  . GLY   A 1 92  ? -12.655 7.600   22.959  1.00 29.83  ? 89  GLY   A CA  1 
ATOM   711  C C   . GLY   A 1 92  ? -13.089 8.950   23.499  1.00 30.85  ? 89  GLY   A C   1 
ATOM   712  O O   . GLY   A 1 92  ? -12.269 9.823   23.805  1.00 33.90  ? 89  GLY   A O   1 
ATOM   713  N N   . PHE   A 1 93  ? -14.404 9.113   23.623  1.00 29.42  ? 90  PHE   A N   1 
ATOM   714  C CA  . PHE   A 1 93  ? -14.992 10.394  24.032  1.00 34.33  ? 90  PHE   A CA  1 
ATOM   715  C C   . PHE   A 1 93  ? -15.045 10.466  25.564  1.00 36.49  ? 90  PHE   A C   1 
ATOM   716  O O   . PHE   A 1 93  ? -16.100 10.465  26.192  1.00 33.37  ? 90  PHE   A O   1 
ATOM   717  C CB  . PHE   A 1 93  ? -16.372 10.553  23.407  1.00 33.39  ? 90  PHE   A CB  1 
ATOM   718  C CG  . PHE   A 1 93  ? -16.752 11.971  23.067  1.00 35.22  ? 90  PHE   A CG  1 
ATOM   719  C CD1 . PHE   A 1 93  ? -16.130 12.647  22.022  1.00 36.71  ? 90  PHE   A CD1 1 
ATOM   720  C CD2 . PHE   A 1 93  ? -17.778 12.602  23.741  1.00 32.34  ? 90  PHE   A CD2 1 
ATOM   721  C CE1 . PHE   A 1 93  ? -16.495 13.948  21.686  1.00 36.17  ? 90  PHE   A CE1 1 
ATOM   722  C CE2 . PHE   A 1 93  ? -18.159 13.902  23.403  1.00 42.04  ? 90  PHE   A CE2 1 
ATOM   723  C CZ  . PHE   A 1 93  ? -17.522 14.579  22.372  1.00 39.14  ? 90  PHE   A CZ  1 
ATOM   724  N N   . GLY   A 1 94  ? -13.856 10.535  26.166  1.00 32.46  ? 91  GLY   A N   1 
ATOM   725  C CA  . GLY   A 1 94  ? -13.768 10.498  27.606  1.00 30.95  ? 91  GLY   A CA  1 
ATOM   726  C C   . GLY   A 1 94  ? -14.040 11.812  28.295  1.00 33.44  ? 91  GLY   A C   1 
ATOM   727  O O   . GLY   A 1 94  ? -14.339 11.811  29.492  1.00 37.84  ? 91  GLY   A O   1 
ATOM   728  N N   . GLY   A 1 95  ? -13.907 12.935  27.585  1.00 38.05  ? 92  GLY   A N   1 
ATOM   729  C CA  . GLY   A 1 95  ? -14.259 14.238  28.135  1.00 36.54  ? 92  GLY   A CA  1 
ATOM   730  C C   . GLY   A 1 95  ? -13.171 14.875  28.988  1.00 37.33  ? 92  GLY   A C   1 
ATOM   731  O O   . GLY   A 1 95  ? -12.090 14.312  29.239  1.00 31.20  ? 92  GLY   A O   1 
ATOM   732  N N   . TRP   A 1 96  ? -13.483 16.094  29.447  1.00 38.74  ? 93  TRP   A N   1 
ATOM   733  C CA  . TRP   A 1 96  ? -12.544 16.940  30.203  1.00 39.16  ? 93  TRP   A CA  1 
ATOM   734  C C   . TRP   A 1 96  ? -12.529 16.526  31.681  1.00 38.83  ? 93  TRP   A C   1 
ATOM   735  O O   . TRP   A 1 96  ? -12.964 17.243  32.587  1.00 42.36  ? 93  TRP   A O   1 
ATOM   736  C CB  . TRP   A 1 96  ? -12.902 18.414  30.041  1.00 41.75  ? 93  TRP   A CB  1 
ATOM   737  C CG  . TRP   A 1 96  ? -12.756 18.932  28.627  1.00 43.86  ? 93  TRP   A CG  1 
ATOM   738  C CD1 . TRP   A 1 96  ? -12.339 18.222  27.532  1.00 41.78  ? 93  TRP   A CD1 1 
ATOM   739  C CD2 . TRP   A 1 96  ? -13.048 20.256  28.154  1.00 44.62  ? 93  TRP   A CD2 1 
ATOM   740  N NE1 . TRP   A 1 96  ? -12.337 19.024  26.415  1.00 40.64  ? 93  TRP   A NE1 1 
ATOM   741  C CE2 . TRP   A 1 96  ? -12.775 20.274  26.764  1.00 43.29  ? 93  TRP   A CE2 1 
ATOM   742  C CE3 . TRP   A 1 96  ? -13.502 21.429  28.768  1.00 43.77  ? 93  TRP   A CE3 1 
ATOM   743  C CZ2 . TRP   A 1 96  ? -12.936 21.418  25.985  1.00 35.92  ? 93  TRP   A CZ2 1 
ATOM   744  C CZ3 . TRP   A 1 96  ? -13.667 22.566  27.988  1.00 41.47  ? 93  TRP   A CZ3 1 
ATOM   745  C CH2 . TRP   A 1 96  ? -13.382 22.550  26.612  1.00 42.00  ? 93  TRP   A CH2 1 
ATOM   746  N N   . ARG   A 1 97  ? -11.990 15.333  31.911  1.00 36.85  ? 94  ARG   A N   1 
ATOM   747  C CA  . ARG   A 1 97  ? -11.936 14.702  33.216  1.00 32.39  ? 94  ARG   A CA  1 
ATOM   748  C C   . ARG   A 1 97  ? -10.577 14.035  33.372  1.00 38.41  ? 94  ARG   A C   1 
ATOM   749  O O   . ARG   A 1 97  ? -10.060 13.426  32.426  1.00 33.17  ? 94  ARG   A O   1 
ATOM   750  C CB  . ARG   A 1 97  ? -13.049 13.659  33.382  1.00 35.21  ? 94  ARG   A CB  1 
ATOM   751  C CG  . ARG   A 1 97  ? -14.459 14.198  33.290  1.00 36.27  ? 94  ARG   A CG  1 
ATOM   752  C CD  . ARG   A 1 97  ? -15.488 13.063  33.471  1.00 39.01  ? 94  ARG   A CD  1 
ATOM   753  N NE  . ARG   A 1 97  ? -15.441 12.059  32.411  1.00 40.91  ? 94  ARG   A NE  1 
ATOM   754  C CZ  . ARG   A 1 97  ? -16.401 11.170  32.184  1.00 38.39  ? 94  ARG   A CZ  1 
ATOM   755  N NH1 . ARG   A 1 97  ? -17.465 11.095  32.956  1.00 42.84  ? 94  ARG   A NH1 1 
ATOM   756  N NH2 . ARG   A 1 97  ? -16.299 10.346  31.145  1.00 36.13  ? 94  ARG   A NH2 1 
ATOM   757  N N   . THR   A 1 98  ? -10.003 14.145  34.570  1.00 37.71  ? 95  THR   A N   1 
ATOM   758  C CA  . THR   A 1 98  ? -8.716  13.506  34.826  1.00 36.74  ? 95  THR   A CA  1 
ATOM   759  C C   . THR   A 1 98  ? -8.851  11.983  34.893  1.00 37.07  ? 95  THR   A C   1 
ATOM   760  O O   . THR   A 1 98  ? -7.943  11.249  34.473  1.00 37.88  ? 95  THR   A O   1 
ATOM   761  C CB  . THR   A 1 98  ? -8.140  14.060  36.129  1.00 43.79  ? 95  THR   A CB  1 
ATOM   762  O OG1 . THR   A 1 98  ? -8.872  13.530  37.243  1.00 42.25  ? 95  THR   A OG1 1 
ATOM   763  C CG2 . THR   A 1 98  ? -8.273  15.576  36.135  1.00 41.43  ? 95  THR   A CG2 1 
ATOM   764  N N   . HIS   A 1 99  ? -9.965  11.491  35.430  1.00 32.42  ? 96  HIS   A N   1 
ATOM   765  C CA  . HIS   A 1 99  ? -10.199 10.060  35.588  1.00 33.75  ? 96  HIS   A CA  1 
ATOM   766  C C   . HIS   A 1 99  ? -11.678 9.791   35.363  1.00 32.66  ? 96  HIS   A C   1 
ATOM   767  O O   . HIS   A 1 99  ? -12.514 10.686  35.507  1.00 34.24  ? 96  HIS   A O   1 
ATOM   768  C CB  . HIS   A 1 99  ? -9.789  9.554   36.987  1.00 34.86  ? 96  HIS   A CB  1 
ATOM   769  C CG  . HIS   A 1 99  ? -8.352  9.802   37.330  1.00 33.15  ? 96  HIS   A CG  1 
ATOM   770  N ND1 . HIS   A 1 99  ? -7.876  11.044  37.693  1.00 35.90  ? 96  HIS   A ND1 1 
ATOM   771  C CD2 . HIS   A 1 99  ? -7.283  8.969   37.346  1.00 31.70  ? 96  HIS   A CD2 1 
ATOM   772  C CE1 . HIS   A 1 99  ? -6.576  10.967  37.918  1.00 35.94  ? 96  HIS   A CE1 1 
ATOM   773  N NE2 . HIS   A 1 99  ? -6.191  9.718   37.713  1.00 32.94  ? 96  HIS   A NE2 1 
ATOM   774  N N   . LEU   A 1 100 ? -12.000 8.548   35.012  1.00 31.40  ? 97  LEU   A N   1 
ATOM   775  C CA  . LEU   A 1 100 ? -13.384 8.177   34.750  1.00 32.55  ? 97  LEU   A CA  1 
ATOM   776  C C   . LEU   A 1 100 ? -13.491 6.663   34.711  1.00 34.14  ? 97  LEU   A C   1 
ATOM   777  O O   . LEU   A 1 100 ? -12.495 5.948   34.542  1.00 29.78  ? 97  LEU   A O   1 
ATOM   778  C CB  . LEU   A 1 100 ? -13.900 8.760   33.430  1.00 35.07  ? 97  LEU   A CB  1 
ATOM   779  C CG  . LEU   A 1 100 ? -13.081 8.280   32.226  1.00 31.35  ? 97  LEU   A CG  1 
ATOM   780  C CD1 . LEU   A 1 100 ? -13.914 7.439   31.312  1.00 31.24  ? 97  LEU   A CD1 1 
ATOM   781  C CD2 . LEU   A 1 100 ? -12.511 9.447   31.497  1.00 34.27  ? 97  LEU   A CD2 1 
ATOM   782  N N   . VAL   A 1 101 ? -14.726 6.191   34.864  1.00 34.71  ? 98  VAL   A N   1 
ATOM   783  C CA  . VAL   A 1 101 ? -15.071 4.781   34.775  1.00 36.68  ? 98  VAL   A CA  1 
ATOM   784  C C   . VAL   A 1 101 ? -15.985 4.619   33.576  1.00 36.06  ? 98  VAL   A C   1 
ATOM   785  O O   . VAL   A 1 101 ? -16.848 5.469   33.332  1.00 40.20  ? 98  VAL   A O   1 
ATOM   786  C CB  . VAL   A 1 101 ? -15.752 4.279   36.069  1.00 39.20  ? 98  VAL   A CB  1 
ATOM   787  C CG1 . VAL   A 1 101 ? -16.277 2.848   35.904  1.00 36.99  ? 98  VAL   A CG1 1 
ATOM   788  C CG2 . VAL   A 1 101 ? -14.790 4.352   37.244  1.00 35.33  ? 98  VAL   A CG2 1 
ATOM   789  N N   . SER   A 1 102 ? -15.803 3.533   32.833  1.00 35.42  ? 99  SER   A N   1 
ATOM   790  C CA  . SER   A 1 102 ? -16.582 3.294   31.625  1.00 41.26  ? 99  SER   A CA  1 
ATOM   791  C C   . SER   A 1 102 ? -16.262 1.891   31.138  1.00 43.12  ? 99  SER   A C   1 
ATOM   792  O O   . SER   A 1 102 ? -15.158 1.385   31.370  1.00 45.52  ? 99  SER   A O   1 
ATOM   793  C CB  . SER   A 1 102 ? -16.263 4.350   30.538  1.00 45.90  ? 99  SER   A CB  1 
ATOM   794  O OG  . SER   A 1 102 ? -16.820 4.049   29.266  1.00 40.40  ? 99  SER   A OG  1 
ATOM   795  N N   . ASP   A 1 103 ? -17.236 1.259   30.484  1.00 39.15  ? 100 ASP   A N   1 
ATOM   796  C CA  . ASP   A 1 103 ? -16.986 -0.026  29.846  1.00 42.45  ? 100 ASP   A CA  1 
ATOM   797  C C   . ASP   A 1 103 ? -16.547 0.118   28.390  1.00 44.15  ? 100 ASP   A C   1 
ATOM   798  O O   . ASP   A 1 103 ? -16.215 -0.887  27.749  1.00 40.73  ? 100 ASP   A O   1 
ATOM   799  C CB  . ASP   A 1 103 ? -18.224 -0.914  29.940  1.00 46.47  ? 100 ASP   A CB  1 
ATOM   800  C CG  . ASP   A 1 103 ? -19.469 -0.269  29.318  1.00 55.06  ? 100 ASP   A CG  1 
ATOM   801  O OD1 . ASP   A 1 103 ? -19.355 0.720   28.540  1.00 53.12  ? 100 ASP   A OD1 1 
ATOM   802  O OD2 . ASP   A 1 103 ? -20.575 -0.769  29.618  1.00 56.33  ? 100 ASP   A OD2 1 
ATOM   803  N N   . GLY   A 1 104 ? -16.516 1.337   27.859  1.00 41.27  ? 101 GLY   A N   1 
ATOM   804  C CA  . GLY   A 1 104 ? -15.995 1.526   26.521  1.00 41.71  ? 101 GLY   A CA  1 
ATOM   805  C C   . GLY   A 1 104 ? -16.910 1.044   25.423  1.00 44.83  ? 101 GLY   A C   1 
ATOM   806  O O   . GLY   A 1 104 ? -16.464 0.851   24.286  1.00 39.76  ? 101 GLY   A O   1 
ATOM   807  N N   . LYS   A 1 105 ? -18.152 0.832   25.730  1.00 47.53  ? 102 LYS   A N   1 
ATOM   808  C CA  . LYS   A 1 105 ? -19.148 0.378   24.776  1.00 49.73  ? 102 LYS   A CA  1 
ATOM   809  C C   . LYS   A 1 105 ? -19.779 1.578   24.065  1.00 43.92  ? 102 LYS   A C   1 
ATOM   810  O O   . LYS   A 1 105 ? -19.767 2.696   24.591  1.00 44.76  ? 102 LYS   A O   1 
ATOM   811  C CB  . LYS   A 1 105 ? -20.226 -0.440  25.489  1.00 45.86  ? 102 LYS   A CB  1 
ATOM   812  C CG  . LYS   A 1 105 ? -19.759 -1.803  25.974  1.00 44.07  ? 102 LYS   A CG  1 
ATOM   813  C CD  . LYS   A 1 105 ? -20.924 -2.611  26.529  1.00 45.99  ? 102 LYS   A CD  1 
ATOM   814  C CE  . LYS   A 1 105 ? -20.456 -3.767  27.394  1.00 48.75  ? 102 LYS   A CE  1 
ATOM   815  N NZ  . LYS   A 1 105 ? -20.248 -5.016  26.624  1.00 51.93  ? 102 LYS   A NZ  1 
ATOM   816  N N   . PRO   A 1 106 ? -20.299 1.398   22.853  1.00 42.00  ? 103 PRO   A N   1 
ATOM   817  C CA  . PRO   A 1 106 ? -20.950 2.524   22.166  1.00 41.27  ? 103 PRO   A CA  1 
ATOM   818  C C   . PRO   A 1 106 ? -22.072 3.086   23.024  1.00 43.38  ? 103 PRO   A C   1 
ATOM   819  O O   . PRO   A 1 106 ? -22.871 2.337   23.586  1.00 42.66  ? 103 PRO   A O   1 
ATOM   820  C CB  . PRO   A 1 106 ? -21.478 1.895   20.868  1.00 38.19  ? 103 PRO   A CB  1 
ATOM   821  C CG  . PRO   A 1 106 ? -20.640 0.646   20.649  1.00 33.08  ? 103 PRO   A CG  1 
ATOM   822  C CD  . PRO   A 1 106 ? -20.247 0.168   22.032  1.00 42.48  ? 103 PRO   A CD  1 
ATOM   823  N N   . LYS   A 1 107 ? -22.118 4.414   23.139  1.00 42.05  ? 104 LYS   A N   1 
ATOM   824  C CA  . LYS   A 1 107 ? -23.143 5.084   23.931  1.00 46.57  ? 104 LYS   A CA  1 
ATOM   825  C C   . LYS   A 1 107 ? -23.834 6.157   23.109  1.00 49.27  ? 104 LYS   A C   1 
ATOM   826  O O   . LYS   A 1 107 ? -23.192 6.881   22.342  1.00 51.29  ? 104 LYS   A O   1 
ATOM   827  C CB  . LYS   A 1 107 ? -22.571 5.716   25.210  1.00 50.23  ? 104 LYS   A CB  1 
ATOM   828  C CG  . LYS   A 1 107 ? -22.119 4.698   26.238  1.00 52.42  ? 104 LYS   A CG  1 
ATOM   829  C CD  . LYS   A 1 107 ? -21.341 5.357   27.365  1.00 56.17  ? 104 LYS   A CD  1 
ATOM   830  C CE  . LYS   A 1 107 ? -20.147 4.497   27.787  1.00 61.47  ? 104 LYS   A CE  1 
ATOM   831  N NZ  . LYS   A 1 107 ? -18.838 4.970   27.205  1.00 53.53  ? 104 LYS   A NZ  1 
ATOM   832  N N   . LEU   A 1 108 ? -25.141 6.265   23.286  1.00 50.99  ? 105 LEU   A N   1 
ATOM   833  C CA  . LEU   A 1 108 ? -25.930 7.238   22.556  1.00 48.59  ? 105 LEU   A CA  1 
ATOM   834  C C   . LEU   A 1 108 ? -25.869 8.600   23.179  1.00 49.40  ? 105 LEU   A C   1 
ATOM   835  O O   . LEU   A 1 108 ? -25.899 8.743   24.382  1.00 57.95  ? 105 LEU   A O   1 
ATOM   836  C CB  . LEU   A 1 108 ? -27.386 6.759   22.496  1.00 48.27  ? 105 LEU   A CB  1 
ATOM   837  C CG  . LEU   A 1 108 ? -28.548 7.533   21.871  1.00 53.16  ? 105 LEU   A CG  1 
ATOM   838  C CD1 . LEU   A 1 108 ? -28.376 7.755   20.380  1.00 51.64  ? 105 LEU   A CD1 1 
ATOM   839  C CD2 . LEU   A 1 108 ? -29.904 6.940   22.195  1.00 50.35  ? 105 LEU   A CD2 1 
ATOM   840  N N   . TRP   A 1 109 ? -25.788 9.608   22.348  1.00 50.85  ? 106 TRP   A N   1 
ATOM   841  C CA  . TRP   A 1 109 ? -25.755 10.989  22.830  1.00 51.62  ? 106 TRP   A CA  1 
ATOM   842  C C   . TRP   A 1 109 ? -27.195 11.461  22.976  1.00 55.67  ? 106 TRP   A C   1 
ATOM   843  O O   . TRP   A 1 109 ? -27.802 11.958  22.023  1.00 58.11  ? 106 TRP   A O   1 
ATOM   844  C CB  . TRP   A 1 109 ? -24.952 11.883  21.892  1.00 47.61  ? 106 TRP   A CB  1 
ATOM   845  C CG  . TRP   A 1 109 ? -24.839 13.333  22.333  1.00 48.09  ? 106 TRP   A CG  1 
ATOM   846  C CD1 . TRP   A 1 109 ? -24.987 14.426  21.542  1.00 45.96  ? 106 TRP   A CD1 1 
ATOM   847  C CD2 . TRP   A 1 109 ? -24.549 13.835  23.657  1.00 49.44  ? 106 TRP   A CD2 1 
ATOM   848  N NE1 . TRP   A 1 109 ? -24.806 15.575  22.273  1.00 51.13  ? 106 TRP   A NE1 1 
ATOM   849  C CE2 . TRP   A 1 109 ? -24.539 15.243  23.573  1.00 46.84  ? 106 TRP   A CE2 1 
ATOM   850  C CE3 . TRP   A 1 109 ? -24.295 13.232  24.898  1.00 50.06  ? 106 TRP   A CE3 1 
ATOM   851  C CZ2 . TRP   A 1 109 ? -24.292 16.062  24.678  1.00 49.54  ? 106 TRP   A CZ2 1 
ATOM   852  C CZ3 . TRP   A 1 109 ? -24.048 14.046  25.996  1.00 47.49  ? 106 TRP   A CZ3 1 
ATOM   853  C CH2 . TRP   A 1 109 ? -24.050 15.447  25.879  1.00 49.70  ? 106 TRP   A CH2 1 
ATOM   854  N N   . GLN   A 1 110 ? -27.714 11.333  24.200  1.00 59.63  ? 107 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 110 ? -29.151 11.420  24.462  1.00 60.10  ? 107 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 110 ? -29.716 12.786  24.094  1.00 64.86  ? 107 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 110 ? -30.746 12.884  23.414  1.00 67.29  ? 107 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 110 ? -29.418 11.116  25.942  1.00 63.26  ? 107 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 110 ? -29.129 9.676   26.369  1.00 64.66  ? 107 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 110 ? -30.309 8.748   26.101  1.00 72.89  ? 107 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 110 ? -31.408 9.207   25.762  1.00 70.38  ? 107 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 110 ? -30.091 7.439   26.255  1.00 62.87  ? 107 GLN   A NE2 1 
ATOM   863  N N   . THR   A 1 111 ? -29.064 13.854  24.549  1.00 59.43  ? 108 THR   A N   1 
ATOM   864  C CA  . THR   A 1 111 ? -29.600 15.199  24.433  1.00 58.65  ? 108 THR   A CA  1 
ATOM   865  C C   . THR   A 1 111 ? -29.102 15.932  23.195  1.00 59.30  ? 108 THR   A C   1 
ATOM   866  O O   . THR   A 1 111 ? -29.153 17.170  23.155  1.00 63.01  ? 108 THR   A O   1 
ATOM   867  C CB  . THR   A 1 111 ? -29.259 15.990  25.691  1.00 61.14  ? 108 THR   A CB  1 
ATOM   868  O OG1 . THR   A 1 111 ? -27.845 16.227  25.732  1.00 55.22  ? 108 THR   A OG1 1 
ATOM   869  C CG2 . THR   A 1 111 ? -29.679 15.192  26.911  1.00 55.08  ? 108 THR   A CG2 1 
ATOM   870  N N   . GLY   A 1 112 ? -28.623 15.202  22.187  1.00 58.69  ? 109 GLY   A N   1 
ATOM   871  C CA  . GLY   A 1 112 ? -28.144 15.830  20.979  1.00 57.71  ? 109 GLY   A CA  1 
ATOM   872  C C   . GLY   A 1 112 ? -29.205 15.938  19.901  1.00 58.76  ? 109 GLY   A C   1 
ATOM   873  O O   . GLY   A 1 112 ? -30.232 15.267  19.932  1.00 65.96  ? 109 GLY   A O   1 
ATOM   874  N N   . THR   A 1 113 ? -28.917 16.791  18.921  1.00 57.15  ? 110 THR   A N   1 
ATOM   875  C CA  . THR   A 1 113 ? -29.869 17.058  17.848  1.00 62.46  ? 110 THR   A CA  1 
ATOM   876  C C   . THR   A 1 113 ? -30.182 15.809  17.018  1.00 63.34  ? 110 THR   A C   1 
ATOM   877  O O   . THR   A 1 113 ? -31.287 15.686  16.476  1.00 63.71  ? 110 THR   A O   1 
ATOM   878  C CB  . THR   A 1 113 ? -29.312 18.180  16.966  1.00 67.01  ? 110 THR   A CB  1 
ATOM   879  O OG1 . THR   A 1 113 ? -28.978 19.305  17.796  1.00 62.73  ? 110 THR   A OG1 1 
ATOM   880  C CG2 . THR   A 1 113 ? -30.322 18.592  15.883  1.00 56.11  ? 110 THR   A CG2 1 
ATOM   881  N N   . PHE   A 1 114 ? -29.240 14.888  16.908  1.00 63.75  ? 111 PHE   A N   1 
ATOM   882  C CA  . PHE   A 1 114 ? -29.439 13.681  16.122  1.00 57.96  ? 111 PHE   A CA  1 
ATOM   883  C C   . PHE   A 1 114 ? -29.183 12.445  16.954  1.00 52.41  ? 111 PHE   A C   1 
ATOM   884  O O   . PHE   A 1 114 ? -28.499 12.513  17.954  1.00 53.77  ? 111 PHE   A O   1 
ATOM   885  C CB  . PHE   A 1 114 ? -28.490 13.677  14.930  1.00 54.63  ? 111 PHE   A CB  1 
ATOM   886  C CG  . PHE   A 1 114 ? -28.572 14.897  14.077  1.00 56.83  ? 111 PHE   A CG  1 
ATOM   887  C CD1 . PHE   A 1 114 ? -29.539 15.006  13.102  1.00 62.55  ? 111 PHE   A CD1 1 
ATOM   888  C CD2 . PHE   A 1 114 ? -27.665 15.920  14.231  1.00 62.58  ? 111 PHE   A CD2 1 
ATOM   889  C CE1 . PHE   A 1 114 ? -29.611 16.126  12.301  1.00 61.57  ? 111 PHE   A CE1 1 
ATOM   890  C CE2 . PHE   A 1 114 ? -27.732 17.046  13.437  1.00 62.93  ? 111 PHE   A CE2 1 
ATOM   891  C CZ  . PHE   A 1 114 ? -28.708 17.150  12.470  1.00 53.59  ? 111 PHE   A CZ  1 
ATOM   892  N N   . PRO   A 1 115 ? -29.715 11.304  16.533  1.00 53.16  ? 112 PRO   A N   1 
ATOM   893  C CA  . PRO   A 1 115 ? -29.426 10.056  17.251  1.00 48.24  ? 112 PRO   A CA  1 
ATOM   894  C C   . PRO   A 1 115 ? -27.986 9.604   17.057  1.00 53.53  ? 112 PRO   A C   1 
ATOM   895  O O   . PRO   A 1 115 ? -27.728 8.552   16.450  1.00 51.74  ? 112 PRO   A O   1 
ATOM   896  C CB  . PRO   A 1 115 ? -30.393 9.057   16.611  1.00 55.04  ? 112 PRO   A CB  1 
ATOM   897  C CG  . PRO   A 1 115 ? -30.493 9.529   15.196  1.00 51.18  ? 112 PRO   A CG  1 
ATOM   898  C CD  . PRO   A 1 115 ? -30.504 11.055  15.315  1.00 55.92  ? 112 PRO   A CD  1 
ATOM   899  N N   . MET   A 1 116 ? -27.049 10.390  17.573  1.00 48.02  ? 113 MET   A N   1 
ATOM   900  C CA  . MET   A 1 116 ? -25.630 10.064  17.442  1.00 53.38  ? 113 MET   A CA  1 
ATOM   901  C C   . MET   A 1 116 ? -25.143 9.066   18.475  1.00 49.90  ? 113 MET   A C   1 
ATOM   902  O O   . MET   A 1 116 ? -25.489 9.149   19.641  1.00 51.33  ? 113 MET   A O   1 
ATOM   903  C CB  . MET   A 1 116 ? -24.779 11.328  17.511  1.00 46.71  ? 113 MET   A CB  1 
ATOM   904  C CG  . MET   A 1 116 ? -23.290 11.075  17.571  1.00 42.69  ? 113 MET   A CG  1 
ATOM   905  S SD  . MET   A 1 116 ? -22.391 12.623  17.484  1.00 56.13  ? 113 MET   A SD  1 
ATOM   906  C CE  . MET   A 1 116 ? -22.746 13.317  19.089  1.00 54.66  ? 113 MET   A CE  1 
ATOM   907  N N   . VAL   A 1 117 ? -24.337 8.127   18.035  1.00 44.22  ? 114 VAL   A N   1 
ATOM   908  C CA  . VAL   A 1 117 ? -23.807 7.103   18.926  1.00 48.14  ? 114 VAL   A CA  1 
ATOM   909  C C   . VAL   A 1 117 ? -22.295 7.253   18.980  1.00 45.93  ? 114 VAL   A C   1 
ATOM   910  O O   . VAL   A 1 117 ? -21.604 6.979   17.988  1.00 49.98  ? 114 VAL   A O   1 
ATOM   911  C CB  . VAL   A 1 117 ? -24.190 5.685   18.482  1.00 48.52  ? 114 VAL   A CB  1 
ATOM   912  C CG1 . VAL   A 1 117 ? -23.541 4.664   19.413  1.00 45.61  ? 114 VAL   A CG1 1 
ATOM   913  C CG2 . VAL   A 1 117 ? -25.685 5.532   18.489  1.00 45.05  ? 114 VAL   A CG2 1 
ATOM   914  N N   . PHE   A 1 118 ? -21.781 7.671   20.134  1.00 38.98  ? 115 PHE   A N   1 
ATOM   915  C CA  . PHE   A 1 118 ? -20.343 7.783   20.315  1.00 41.15  ? 115 PHE   A CA  1 
ATOM   916  C C   . PHE   A 1 118 ? -19.695 6.405   20.165  1.00 42.98  ? 115 PHE   A C   1 
ATOM   917  O O   . PHE   A 1 118 ? -20.178 5.433   20.756  1.00 45.86  ? 115 PHE   A O   1 
ATOM   918  C CB  . PHE   A 1 118 ? -20.007 8.357   21.689  1.00 39.67  ? 115 PHE   A CB  1 
ATOM   919  C CG  . PHE   A 1 118 ? -20.415 9.804   21.888  1.00 40.44  ? 115 PHE   A CG  1 
ATOM   920  C CD1 . PHE   A 1 118 ? -19.910 10.819  21.068  1.00 40.59  ? 115 PHE   A CD1 1 
ATOM   921  C CD2 . PHE   A 1 118 ? -21.260 10.155  22.945  1.00 38.98  ? 115 PHE   A CD2 1 
ATOM   922  C CE1 . PHE   A 1 118 ? -20.257 12.171  21.285  1.00 41.42  ? 115 PHE   A CE1 1 
ATOM   923  C CE2 . PHE   A 1 118 ? -21.624 11.502  23.169  1.00 40.51  ? 115 PHE   A CE2 1 
ATOM   924  C CZ  . PHE   A 1 118 ? -21.117 12.512  22.333  1.00 42.76  ? 115 PHE   A CZ  1 
ATOM   925  N N   . PRO   A 1 119 ? -18.611 6.277   19.399  1.00 38.01  ? 116 PRO   A N   1 
ATOM   926  C CA  . PRO   A 1 119 ? -18.052 4.946   19.141  1.00 36.80  ? 116 PRO   A CA  1 
ATOM   927  C C   . PRO   A 1 119 ? -17.559 4.261   20.415  1.00 37.99  ? 116 PRO   A C   1 
ATOM   928  O O   . PRO   A 1 119 ? -17.267 4.896   21.430  1.00 37.08  ? 116 PRO   A O   1 
ATOM   929  C CB  . PRO   A 1 119 ? -16.891 5.235   18.176  1.00 29.94  ? 116 PRO   A CB  1 
ATOM   930  C CG  . PRO   A 1 119 ? -16.525 6.653   18.461  1.00 31.51  ? 116 PRO   A CG  1 
ATOM   931  C CD  . PRO   A 1 119 ? -17.814 7.341   18.758  1.00 31.50  ? 116 PRO   A CD  1 
ATOM   932  N N   . ALA   A 1 120 ? -17.489 2.931   20.347  1.00 39.35  ? 117 ALA   A N   1 
ATOM   933  C CA  . ALA   A 1 120 ? -16.730 2.155   21.323  1.00 41.84  ? 117 ALA   A CA  1 
ATOM   934  C C   . ALA   A 1 120 ? -15.298 2.657   21.384  1.00 35.69  ? 117 ALA   A C   1 
ATOM   935  O O   . ALA   A 1 120 ? -14.725 3.034   20.362  1.00 33.74  ? 117 ALA   A O   1 
ATOM   936  C CB  . ALA   A 1 120 ? -16.722 0.671   20.942  1.00 35.86  ? 117 ALA   A CB  1 
ATOM   937  N N   . TYR   A 1 121 ? -14.728 2.662   22.593  1.00 36.01  ? 118 TYR   A N   1 
ATOM   938  C CA  . TYR   A 1 121 ? -13.331 3.049   22.757  1.00 35.91  ? 118 TYR   A CA  1 
ATOM   939  C C   . TYR   A 1 121 ? -12.470 2.162   21.869  1.00 34.64  ? 118 TYR   A C   1 
ATOM   940  O O   . TYR   A 1 121 ? -12.790 0.990   21.638  1.00 34.97  ? 118 TYR   A O   1 
ATOM   941  C CB  . TYR   A 1 121 ? -12.868 2.923   24.221  1.00 32.11  ? 118 TYR   A CB  1 
ATOM   942  C CG  . TYR   A 1 121 ? -13.500 3.891   25.218  1.00 34.70  ? 118 TYR   A CG  1 
ATOM   943  C CD1 . TYR   A 1 121 ? -14.441 4.823   24.810  1.00 31.35  ? 118 TYR   A CD1 1 
ATOM   944  C CD2 . TYR   A 1 121 ? -13.140 3.872   26.577  1.00 36.23  ? 118 TYR   A CD2 1 
ATOM   945  C CE1 . TYR   A 1 121 ? -15.021 5.706   25.716  1.00 33.76  ? 118 TYR   A CE1 1 
ATOM   946  C CE2 . TYR   A 1 121 ? -13.710 4.760   27.496  1.00 35.18  ? 118 TYR   A CE2 1 
ATOM   947  C CZ  . TYR   A 1 121 ? -14.657 5.678   27.052  1.00 40.41  ? 118 TYR   A CZ  1 
ATOM   948  O OH  . TYR   A 1 121 ? -15.252 6.581   27.921  1.00 38.92  ? 118 TYR   A OH  1 
ATOM   949  N N   . ARG   A 1 122 ? -11.369 2.729   21.377  1.00 30.36  ? 119 ARG   A N   1 
ATOM   950  C CA  . ARG   A 1 122 ? -10.503 2.085   20.397  1.00 32.19  ? 119 ARG   A CA  1 
ATOM   951  C C   . ARG   A 1 122 ? -9.128  1.852   21.001  1.00 33.43  ? 119 ARG   A C   1 
ATOM   952  O O   . ARG   A 1 122 ? -8.523  2.782   21.543  1.00 33.55  ? 119 ARG   A O   1 
ATOM   953  C CB  . ARG   A 1 122 ? -10.384 2.954   19.132  1.00 32.61  ? 119 ARG   A CB  1 
ATOM   954  C CG  . ARG   A 1 122 ? -9.275  2.556   18.178  1.00 34.45  ? 119 ARG   A CG  1 
ATOM   955  C CD  . ARG   A 1 122 ? -9.299  3.410   16.898  1.00 36.56  ? 119 ARG   A CD  1 
ATOM   956  N NE  . ARG   A 1 122 ? -9.051  4.841   17.104  1.00 37.58  ? 119 ARG   A NE  1 
ATOM   957  C CZ  . ARG   A 1 122 ? -7.933  5.459   16.728  1.00 36.10  ? 119 ARG   A CZ  1 
ATOM   958  N NH1 . ARG   A 1 122 ? -6.921  4.790   16.185  1.00 31.25  ? 119 ARG   A NH1 1 
ATOM   959  N NH2 . ARG   A 1 122 ? -7.835  6.780   16.877  1.00 27.70  ? 119 ARG   A NH2 1 
ATOM   960  N N   . LYS   A 1 123 ? -8.623  0.628   20.877  1.00 34.43  ? 120 LYS   A N   1 
ATOM   961  C CA  . LYS   A 1 123 ? -7.309  0.306   21.412  1.00 31.99  ? 120 LYS   A CA  1 
ATOM   962  C C   . LYS   A 1 123 ? -6.216  0.928   20.560  1.00 32.01  ? 120 LYS   A C   1 
ATOM   963  O O   . LYS   A 1 123 ? -6.246  0.835   19.332  1.00 35.57  ? 120 LYS   A O   1 
ATOM   964  C CB  . LYS   A 1 123 ? -7.106  -1.208  21.478  1.00 31.27  ? 120 LYS   A CB  1 
ATOM   965  C CG  . LYS   A 1 123 ? -6.065  -1.626  22.521  1.00 36.51  ? 120 LYS   A CG  1 
ATOM   966  C CD  . LYS   A 1 123 ? -5.460  -3.008  22.229  1.00 45.13  ? 120 LYS   A CD  1 
ATOM   967  C CE  . LYS   A 1 123 ? -4.682  -3.565  23.441  1.00 40.90  ? 120 LYS   A CE  1 
ATOM   968  N NZ  . LYS   A 1 123 ? -3.462  -2.780  23.788  1.00 39.51  ? 120 LYS   A NZ  1 
ATOM   969  N N   . LEU   A 1 124 ? -5.235  1.541   21.215  1.00 32.27  ? 121 LEU   A N   1 
ATOM   970  C CA  . LEU   A 1 124 ? -4.098  2.156   20.541  1.00 31.60  ? 121 LEU   A CA  1 
ATOM   971  C C   . LEU   A 1 124 ? -2.878  1.254   20.685  1.00 35.30  ? 121 LEU   A C   1 
ATOM   972  O O   . LEU   A 1 124 ? -2.568  0.786   21.785  1.00 35.94  ? 121 LEU   A O   1 
ATOM   973  C CB  . LEU   A 1 124 ? -3.819  3.548   21.119  1.00 26.37  ? 121 LEU   A CB  1 
ATOM   974  C CG  . LEU   A 1 124 ? -5.039  4.468   21.038  1.00 28.82  ? 121 LEU   A CG  1 
ATOM   975  C CD1 . LEU   A 1 124 ? -4.805  5.796   21.745  1.00 27.82  ? 121 LEU   A CD1 1 
ATOM   976  C CD2 . LEU   A 1 124 ? -5.483  4.686   19.584  1.00 30.66  ? 121 LEU   A CD2 1 
ATOM   977  N N   . ASP   A 1 125 ? -2.183  1.004   19.588  1.00 37.25  ? 122 ASP   A N   1 
ATOM   978  C CA  . ASP   A 1 125 ? -1.033  0.115   19.638  1.00 39.28  ? 122 ASP   A CA  1 
ATOM   979  C C   . ASP   A 1 125 ? 0.249   0.914   19.463  1.00 39.39  ? 122 ASP   A C   1 
ATOM   980  O O   . ASP   A 1 125 ? 0.443   1.568   18.431  1.00 36.00  ? 122 ASP   A O   1 
ATOM   981  C CB  . ASP   A 1 125 ? -1.127  -0.979  18.586  1.00 41.64  ? 122 ASP   A CB  1 
ATOM   982  C CG  . ASP   A 1 125 ? -0.523  -2.256  19.076  1.00 56.62  ? 122 ASP   A CG  1 
ATOM   983  O OD1 . ASP   A 1 125 ? -1.225  -2.979  19.825  1.00 64.54  ? 122 ASP   A OD1 1 
ATOM   984  O OD2 . ASP   A 1 125 ? 0.668   -2.503  18.779  1.00 56.61  ? 122 ASP   A OD2 1 
ATOM   985  N N   . LEU   A 1 126 ? 1.126   0.847   20.470  1.00 38.64  ? 123 LEU   A N   1 
ATOM   986  C CA  . LEU   A 1 126 ? 2.319   1.685   20.475  1.00 34.25  ? 123 LEU   A CA  1 
ATOM   987  C C   . LEU   A 1 126 ? 3.171   1.510   19.220  1.00 36.58  ? 123 LEU   A C   1 
ATOM   988  O O   . LEU   A 1 126 ? 3.893   2.444   18.846  1.00 36.36  ? 123 LEU   A O   1 
ATOM   989  C CB  . LEU   A 1 126 ? 3.133   1.411   21.735  1.00 27.87  ? 123 LEU   A CB  1 
ATOM   990  C CG  . LEU   A 1 126 ? 2.433   2.031   22.952  1.00 32.92  ? 123 LEU   A CG  1 
ATOM   991  C CD1 . LEU   A 1 126 ? 3.095   1.680   24.266  1.00 23.83  ? 123 LEU   A CD1 1 
ATOM   992  C CD2 . LEU   A 1 126 ? 2.321   3.549   22.791  1.00 29.09  ? 123 LEU   A CD2 1 
ATOM   993  N N   . ARG   A 1 127 ? 3.069   0.364   18.534  1.00 36.80  ? 124 ARG   A N   1 
ATOM   994  C CA  . ARG   A 1 127 ? 3.918   0.128   17.366  1.00 37.20  ? 124 ARG   A CA  1 
ATOM   995  C C   . ARG   A 1 127 ? 3.658   1.143   16.263  1.00 34.13  ? 124 ARG   A C   1 
ATOM   996  O O   . ARG   A 1 127 ? 4.572   1.464   15.503  1.00 34.57  ? 124 ARG   A O   1 
ATOM   997  C CB  . ARG   A 1 127 ? 3.725   -1.298  16.830  1.00 39.72  ? 124 ARG   A CB  1 
ATOM   998  C CG  . ARG   A 1 127 ? 2.482   -1.488  15.959  1.00 47.47  ? 124 ARG   A CG  1 
ATOM   999  C CD  . ARG   A 1 127 ? 2.234   -2.954  15.577  1.00 53.26  ? 124 ARG   A CD  1 
ATOM   1000 N NE  . ARG   A 1 127 ? 1.898   -3.745  16.756  1.00 57.47  ? 124 ARG   A NE  1 
ATOM   1001 C CZ  . ARG   A 1 127 ? 1.421   -4.985  16.745  1.00 57.45  ? 124 ARG   A CZ  1 
ATOM   1002 N NH1 . ARG   A 1 127 ? 1.211   -5.638  15.613  1.00 63.44  ? 124 ARG   A NH1 1 
ATOM   1003 N NH2 . ARG   A 1 127 ? 1.146   -5.584  17.904  1.00 57.49  ? 124 ARG   A NH2 1 
ATOM   1004 N N   . HIS   A 1 128 ? 2.438   1.686   16.185  1.00 37.02  ? 125 HIS   A N   1 
ATOM   1005 C CA  . HIS   A 1 128 ? 2.080   2.691   15.183  1.00 36.12  ? 125 HIS   A CA  1 
ATOM   1006 C C   . HIS   A 1 128 ? 2.668   4.069   15.444  1.00 33.97  ? 125 HIS   A C   1 
ATOM   1007 O O   . HIS   A 1 128 ? 2.629   4.901   14.542  1.00 37.80  ? 125 HIS   A O   1 
ATOM   1008 C CB  . HIS   A 1 128 ? 0.563   2.851   15.091  1.00 35.94  ? 125 HIS   A CB  1 
ATOM   1009 C CG  . HIS   A 1 128 ? -0.146  1.594   14.731  1.00 34.89  ? 125 HIS   A CG  1 
ATOM   1010 N ND1 . HIS   A 1 128 ? -1.275  1.164   15.393  1.00 45.80  ? 125 HIS   A ND1 1 
ATOM   1011 C CD2 . HIS   A 1 128 ? 0.119   0.661   13.790  1.00 38.52  ? 125 HIS   A CD2 1 
ATOM   1012 C CE1 . HIS   A 1 128 ? -1.673  0.015   14.876  1.00 45.98  ? 125 HIS   A CE1 1 
ATOM   1013 N NE2 . HIS   A 1 128 ? -0.843  -0.312  13.903  1.00 48.00  ? 125 HIS   A NE2 1 
ATOM   1014 N N   . TYR   A 1 129 ? 3.169   4.357   16.637  1.00 37.00  ? 126 TYR   A N   1 
ATOM   1015 C CA  . TYR   A 1 129 ? 3.569   5.713   16.966  1.00 33.92  ? 126 TYR   A CA  1 
ATOM   1016 C C   . TYR   A 1 129 ? 5.064   5.763   17.200  1.00 37.53  ? 126 TYR   A C   1 
ATOM   1017 O O   . TYR   A 1 129 ? 5.674   4.795   17.656  1.00 37.21  ? 126 TYR   A O   1 
ATOM   1018 C CB  . TYR   A 1 129 ? 2.816   6.234   18.201  1.00 34.93  ? 126 TYR   A CB  1 
ATOM   1019 C CG  . TYR   A 1 129 ? 1.329   5.988   18.073  1.00 35.91  ? 126 TYR   A CG  1 
ATOM   1020 C CD1 . TYR   A 1 129 ? 0.535   6.829   17.307  1.00 31.40  ? 126 TYR   A CD1 1 
ATOM   1021 C CD2 . TYR   A 1 129 ? 0.734   4.876   18.658  1.00 34.65  ? 126 TYR   A CD2 1 
ATOM   1022 C CE1 . TYR   A 1 129 ? -0.802  6.596   17.156  1.00 32.44  ? 126 TYR   A CE1 1 
ATOM   1023 C CE2 . TYR   A 1 129 ? -0.620  4.633   18.509  1.00 35.78  ? 126 TYR   A CE2 1 
ATOM   1024 C CZ  . TYR   A 1 129 ? -1.386  5.497   17.749  1.00 33.44  ? 126 TYR   A CZ  1 
ATOM   1025 O OH  . TYR   A 1 129 ? -2.745  5.276   17.581  1.00 35.08  ? 126 TYR   A OH  1 
ATOM   1026 N N   . ASP   A 1 130 ? 5.645   6.902   16.861  1.00 39.43  ? 127 ASP   A N   1 
ATOM   1027 C CA  . ASP   A 1 130 ? 7.050   7.160   17.119  1.00 36.56  ? 127 ASP   A CA  1 
ATOM   1028 C C   . ASP   A 1 130 ? 7.233   8.668   17.172  1.00 31.76  ? 127 ASP   A C   1 
ATOM   1029 O O   . ASP   A 1 130 ? 6.263   9.428   17.233  1.00 32.10  ? 127 ASP   A O   1 
ATOM   1030 C CB  . ASP   A 1 130 ? 7.930   6.493   16.057  1.00 42.59  ? 127 ASP   A CB  1 
ATOM   1031 C CG  . ASP   A 1 130 ? 7.377   6.683   14.649  1.00 49.74  ? 127 ASP   A CG  1 
ATOM   1032 O OD1 . ASP   A 1 130 ? 7.343   7.849   14.174  1.00 48.14  ? 127 ASP   A OD1 1 
ATOM   1033 O OD2 . ASP   A 1 130 ? 6.961   5.660   14.035  1.00 53.46  ? 127 ASP   A OD2 1 
ATOM   1034 N N   . ASP   A 1 131 ? 8.478   9.109   17.129  1.00 34.65  ? 128 ASP   A N   1 
ATOM   1035 C CA  . ASP   A 1 131 ? 8.742   10.536  17.262  1.00 39.48  ? 128 ASP   A CA  1 
ATOM   1036 C C   . ASP   A 1 131 ? 8.133   11.345  16.119  1.00 37.16  ? 128 ASP   A C   1 
ATOM   1037 O O   . ASP   A 1 131 ? 7.691   12.478  16.330  1.00 42.36  ? 128 ASP   A O   1 
ATOM   1038 C CB  . ASP   A 1 131 ? 10.252  10.759  17.375  1.00 43.01  ? 128 ASP   A CB  1 
ATOM   1039 C CG  . ASP   A 1 131 ? 10.835  10.145  18.665  1.00 52.23  ? 128 ASP   A CG  1 
ATOM   1040 O OD1 . ASP   A 1 131 ? 10.037  9.768   19.566  1.00 46.44  ? 128 ASP   A OD1 1 
ATOM   1041 O OD2 . ASP   A 1 131 ? 12.080  10.029  18.773  1.00 53.61  ? 128 ASP   A OD2 1 
ATOM   1042 N N   . ALA   A 1 132 ? 8.071   10.782  14.915  1.00 38.18  ? 129 ALA   A N   1 
ATOM   1043 C CA  . ALA   A 1 132 ? 7.465   11.507  13.806  1.00 37.89  ? 129 ALA   A CA  1 
ATOM   1044 C C   . ALA   A 1 132 ? 5.948   11.513  13.914  1.00 36.86  ? 129 ALA   A C   1 
ATOM   1045 O O   . ALA   A 1 132 ? 5.300   12.513  13.590  1.00 43.10  ? 129 ALA   A O   1 
ATOM   1046 C CB  . ALA   A 1 132 ? 7.897   10.900  12.472  1.00 32.66  ? 129 ALA   A CB  1 
ATOM   1047 N N   . LEU   A 1 133 ? 5.365   10.412  14.368  1.00 35.90  ? 130 LEU   A N   1 
ATOM   1048 C CA  . LEU   A 1 133 ? 3.918   10.274  14.502  1.00 36.05  ? 130 LEU   A CA  1 
ATOM   1049 C C   . LEU   A 1 133 ? 3.602   9.868   15.941  1.00 34.35  ? 130 LEU   A C   1 
ATOM   1050 O O   . LEU   A 1 133 ? 3.278   8.704   16.205  1.00 39.07  ? 130 LEU   A O   1 
ATOM   1051 C CB  . LEU   A 1 133 ? 3.391   9.249   13.495  1.00 30.32  ? 130 LEU   A CB  1 
ATOM   1052 C CG  . LEU   A 1 133 ? 1.970   9.437   12.968  1.00 37.31  ? 130 LEU   A CG  1 
ATOM   1053 C CD1 . LEU   A 1 133 ? 1.723   10.867  12.485  1.00 34.12  ? 130 LEU   A CD1 1 
ATOM   1054 C CD2 . LEU   A 1 133 ? 1.680   8.445   11.870  1.00 39.11  ? 130 LEU   A CD2 1 
ATOM   1055 N N   . PRO   A 1 134 ? 3.700   10.792  16.896  1.00 35.53  ? 131 PRO   A N   1 
ATOM   1056 C CA  . PRO   A 1 134 ? 3.587   10.411  18.315  1.00 34.86  ? 131 PRO   A CA  1 
ATOM   1057 C C   . PRO   A 1 134 ? 2.175   9.990   18.702  1.00 36.45  ? 131 PRO   A C   1 
ATOM   1058 O O   . PRO   A 1 134 ? 1.203   10.184  17.966  1.00 32.64  ? 131 PRO   A O   1 
ATOM   1059 C CB  . PRO   A 1 134 ? 4.016   11.671  19.073  1.00 30.86  ? 131 PRO   A CB  1 
ATOM   1060 C CG  . PRO   A 1 134 ? 3.835   12.772  18.140  1.00 34.03  ? 131 PRO   A CG  1 
ATOM   1061 C CD  . PRO   A 1 134 ? 4.051   12.213  16.742  1.00 37.83  ? 131 PRO   A CD  1 
ATOM   1062 N N   . LEU   A 1 135 ? 2.093   9.404   19.908  1.00 34.58  ? 132 LEU   A N   1 
ATOM   1063 C CA  . LEU   A 1 135 ? 0.844   8.858   20.440  1.00 30.61  ? 132 LEU   A CA  1 
ATOM   1064 C C   . LEU   A 1 135 ? -0.299  9.867   20.387  1.00 30.62  ? 132 LEU   A C   1 
ATOM   1065 O O   . LEU   A 1 135 ? -1.448  9.508   20.106  1.00 34.00  ? 132 LEU   A O   1 
ATOM   1066 C CB  . LEU   A 1 135 ? 1.065   8.401   21.884  1.00 30.81  ? 132 LEU   A CB  1 
ATOM   1067 C CG  . LEU   A 1 135 ? -0.190  8.112   22.714  1.00 32.70  ? 132 LEU   A CG  1 
ATOM   1068 C CD1 . LEU   A 1 135 ? -0.943  6.949   22.056  1.00 29.34  ? 132 LEU   A CD1 1 
ATOM   1069 C CD2 . LEU   A 1 135 ? 0.146   7.797   24.184  1.00 30.05  ? 132 LEU   A CD2 1 
ATOM   1070 N N   . SER   A 1 136 ? -0.013  11.127  20.678  1.00 25.60  ? 133 SER   A N   1 
ATOM   1071 C CA  . SER   A 1 136 ? -1.059  12.129  20.668  1.00 25.53  ? 133 SER   A CA  1 
ATOM   1072 C C   . SER   A 1 136 ? -1.722  12.273  19.298  1.00 31.04  ? 133 SER   A C   1 
ATOM   1073 O O   . SER   A 1 136 ? -2.826  12.817  19.217  1.00 32.26  ? 133 SER   A O   1 
ATOM   1074 C CB  . SER   A 1 136 ? -0.462  13.455  21.122  1.00 31.01  ? 133 SER   A CB  1 
ATOM   1075 O OG  . SER   A 1 136 ? 0.709   13.740  20.366  1.00 36.47  ? 133 SER   A OG  1 
ATOM   1076 N N   . THR   A 1 137 ? -1.086  11.802  18.217  1.00 30.17  ? 134 THR   A N   1 
ATOM   1077 C CA  . THR   A 1 137 ? -1.718  11.866  16.905  1.00 30.41  ? 134 THR   A CA  1 
ATOM   1078 C C   . THR   A 1 137 ? -2.967  11.011  16.820  1.00 30.90  ? 134 THR   A C   1 
ATOM   1079 O O   . THR   A 1 137 ? -3.708  11.147  15.847  1.00 29.51  ? 134 THR   A O   1 
ATOM   1080 C CB  . THR   A 1 137 ? -0.769  11.437  15.779  1.00 32.90  ? 134 THR   A CB  1 
ATOM   1081 O OG1 . THR   A 1 137 ? -0.342  10.080  15.974  1.00 31.55  ? 134 THR   A OG1 1 
ATOM   1082 C CG2 . THR   A 1 137 ? 0.431   12.380  15.688  1.00 30.78  ? 134 THR   A CG2 1 
ATOM   1083 N N   . ALA   A 1 138 ? -3.228  10.152  17.811  1.00 32.88  ? 135 ALA   A N   1 
ATOM   1084 C CA  . ALA   A 1 138 ? -4.507  9.451   17.863  1.00 33.65  ? 135 ALA   A CA  1 
ATOM   1085 C C   . ALA   A 1 138 ? -5.680  10.403  18.079  1.00 30.99  ? 135 ALA   A C   1 
ATOM   1086 O O   . ALA   A 1 138 ? -6.836  9.988   17.921  1.00 31.74  ? 135 ALA   A O   1 
ATOM   1087 C CB  . ALA   A 1 138 ? -4.480  8.374   18.954  1.00 28.63  ? 135 ALA   A CB  1 
ATOM   1088 N N   . LEU   A 1 139 ? -5.415  11.659  18.423  1.00 30.20  ? 136 LEU   A N   1 
ATOM   1089 C CA  . LEU   A 1 139 ? -6.443  12.684  18.500  1.00 29.46  ? 136 LEU   A CA  1 
ATOM   1090 C C   . LEU   A 1 139 ? -6.423  13.613  17.294  1.00 31.06  ? 136 LEU   A C   1 
ATOM   1091 O O   . LEU   A 1 139 ? -7.267  14.514  17.200  1.00 31.25  ? 136 LEU   A O   1 
ATOM   1092 C CB  . LEU   A 1 139 ? -6.269  13.497  19.791  1.00 27.45  ? 136 LEU   A CB  1 
ATOM   1093 C CG  . LEU   A 1 139 ? -6.569  12.725  21.074  1.00 31.21  ? 136 LEU   A CG  1 
ATOM   1094 C CD1 . LEU   A 1 139 ? -6.346  13.598  22.337  1.00 27.57  ? 136 LEU   A CD1 1 
ATOM   1095 C CD2 . LEU   A 1 139 ? -7.981  12.147  21.016  1.00 26.51  ? 136 LEU   A CD2 1 
ATOM   1096 N N   . GLY   A 1 140 ? -5.471  13.427  16.383  1.00 29.45  ? 137 GLY   A N   1 
ATOM   1097 C CA  . GLY   A 1 140 ? -5.307  14.321  15.254  1.00 28.61  ? 137 GLY   A CA  1 
ATOM   1098 C C   . GLY   A 1 140 ? -5.237  13.582  13.935  1.00 30.36  ? 137 GLY   A C   1 
ATOM   1099 O O   . GLY   A 1 140 ? -6.228  12.988  13.491  1.00 27.88  ? 137 GLY   A O   1 
ATOM   1100 N N   . VAL   A 1 141 ? -4.057  13.597  13.310  1.00 27.15  ? 138 VAL   A N   1 
ATOM   1101 C CA  . VAL   A 1 141 ? -3.924  13.058  11.958  1.00 32.07  ? 138 VAL   A CA  1 
ATOM   1102 C C   . VAL   A 1 141 ? -4.170  11.549  11.928  1.00 32.82  ? 138 VAL   A C   1 
ATOM   1103 O O   . VAL   A 1 141 ? -4.622  11.006  10.912  1.00 31.67  ? 138 VAL   A O   1 
ATOM   1104 C CB  . VAL   A 1 141 ? -2.542  13.420  11.385  1.00 34.85  ? 138 VAL   A CB  1 
ATOM   1105 C CG1 . VAL   A 1 141 ? -1.442  12.783  12.224  1.00 32.05  ? 138 VAL   A CG1 1 
ATOM   1106 C CG2 . VAL   A 1 141 ? -2.439  12.978  9.930   1.00 33.35  ? 138 VAL   A CG2 1 
ATOM   1107 N N   . MET   A 1 142 ? -3.864  10.845  13.018  1.00 29.03  ? 139 MET   A N   1 
ATOM   1108 C CA  . MET   A 1 142 ? -4.232  9.446   13.173  1.00 25.96  ? 139 MET   A CA  1 
ATOM   1109 C C   . MET   A 1 142 ? -5.478  9.294   14.025  1.00 27.13  ? 139 MET   A C   1 
ATOM   1110 O O   . MET   A 1 142 ? -5.635  8.291   14.729  1.00 31.11  ? 139 MET   A O   1 
ATOM   1111 C CB  . MET   A 1 142 ? -3.082  8.641   13.773  1.00 26.10  ? 139 MET   A CB  1 
ATOM   1112 C CG  . MET   A 1 142 ? -1.820  8.605   12.937  1.00 31.95  ? 139 MET   A CG  1 
ATOM   1113 S SD  . MET   A 1 142 ? -1.995  7.695   11.381  1.00 37.51  ? 139 MET   A SD  1 
ATOM   1114 C CE  . MET   A 1 142 ? -2.011  9.059   10.225  1.00 39.23  ? 139 MET   A CE  1 
ATOM   1115 N N   . GLY   A 1 143 ? -6.356  10.288  14.001  1.00 28.90  ? 140 GLY   A N   1 
ATOM   1116 C CA  . GLY   A 1 143 ? -7.605  10.206  14.735  1.00 28.51  ? 140 GLY   A CA  1 
ATOM   1117 C C   . GLY   A 1 143 ? -8.798  10.697  13.941  1.00 28.21  ? 140 GLY   A C   1 
ATOM   1118 O O   . GLY   A 1 143 ? -8.840  10.568  12.716  1.00 28.60  ? 140 GLY   A O   1 
ATOM   1119 N N   . GLY   A 1 144 ? -9.775  11.267  14.637  1.00 29.56  ? 141 GLY   A N   1 
ATOM   1120 C CA  . GLY   A 1 144 ? -10.939 11.837  14.010  1.00 28.94  ? 141 GLY   A CA  1 
ATOM   1121 C C   . GLY   A 1 144 ? -10.592 12.723  12.830  1.00 34.18  ? 141 GLY   A C   1 
ATOM   1122 O O   . GLY   A 1 144 ? -11.014 12.475  11.696  1.00 31.06  ? 141 GLY   A O   1 
ATOM   1123 N N   . PRO   A 1 145 ? -9.812  13.780  13.076  1.00 31.83  ? 142 PRO   A N   1 
ATOM   1124 C CA  . PRO   A 1 145 ? -9.512  14.729  11.985  1.00 24.20  ? 142 PRO   A CA  1 
ATOM   1125 C C   . PRO   A 1 145 ? -8.859  14.081  10.774  1.00 33.04  ? 142 PRO   A C   1 
ATOM   1126 O O   . PRO   A 1 145 ? -9.278  14.327  9.630   1.00 33.55  ? 142 PRO   A O   1 
ATOM   1127 C CB  . PRO   A 1 145 ? -8.597  15.755  12.666  1.00 32.11  ? 142 PRO   A CB  1 
ATOM   1128 C CG  . PRO   A 1 145 ? -8.994  15.718  14.113  1.00 29.33  ? 142 PRO   A CG  1 
ATOM   1129 C CD  . PRO   A 1 145 ? -9.412  14.290  14.402  1.00 27.82  ? 142 PRO   A CD  1 
ATOM   1130 N N   . GLY   A 1 146 ? -7.835  13.256  10.979  1.00 32.64  ? 143 GLY   A N   1 
ATOM   1131 C CA  . GLY   A 1 146 ? -7.248  12.566  9.847   1.00 27.39  ? 143 GLY   A CA  1 
ATOM   1132 C C   . GLY   A 1 146 ? -8.257  11.690  9.127   1.00 29.00  ? 143 GLY   A C   1 
ATOM   1133 O O   . GLY   A 1 146 ? -8.268  11.619  7.897   1.00 32.00  ? 143 GLY   A O   1 
ATOM   1134 N N   . MET   A 1 147 ? -9.120  11.011  9.886   1.00 30.25  ? 144 MET   A N   1 
ATOM   1135 C CA  . MET   A 1 147 ? -10.069 10.076  9.287   1.00 27.33  ? 144 MET   A CA  1 
ATOM   1136 C C   . MET   A 1 147 ? -11.094 10.823  8.443   1.00 27.91  ? 144 MET   A C   1 
ATOM   1137 O O   . MET   A 1 147 ? -11.500 10.343  7.379   1.00 26.91  ? 144 MET   A O   1 
ATOM   1138 C CB  . MET   A 1 147 ? -10.747 9.249   10.391  1.00 26.93  ? 144 MET   A CB  1 
ATOM   1139 C CG  . MET   A 1 147 ? -11.722 8.165   9.904   1.00 29.65  ? 144 MET   A CG  1 
ATOM   1140 S SD  . MET   A 1 147 ? -10.937 6.809   8.954   1.00 33.19  ? 144 MET   A SD  1 
ATOM   1141 C CE  . MET   A 1 147 ? -10.352 5.732   10.270  1.00 31.76  ? 144 MET   A CE  1 
ATOM   1142 N N   . THR   A 1 148 ? -11.492 12.015  8.900   1.00 25.50  ? 145 THR   A N   1 
ATOM   1143 C CA  . THR   A 1 148 ? -12.410 12.871  8.158   1.00 27.31  ? 145 THR   A CA  1 
ATOM   1144 C C   . THR   A 1 148 ? -11.817 13.291  6.822   1.00 29.22  ? 145 THR   A C   1 
ATOM   1145 O O   . THR   A 1 148 ? -12.485 13.240  5.780   1.00 24.27  ? 145 THR   A O   1 
ATOM   1146 C CB  . THR   A 1 148 ? -12.717 14.113  8.988   1.00 27.33  ? 145 THR   A CB  1 
ATOM   1147 O OG1 . THR   A 1 148 ? -13.158 13.714  10.289  1.00 28.04  ? 145 THR   A OG1 1 
ATOM   1148 C CG2 . THR   A 1 148 ? -13.778 14.951  8.312   1.00 25.23  ? 145 THR   A CG2 1 
ATOM   1149 N N   . ALA   A 1 149 ? -10.566 13.751  6.854   1.00 25.84  ? 146 ALA   A N   1 
ATOM   1150 C CA  . ALA   A 1 149 ? -9.890  14.194  5.652   1.00 20.96  ? 146 ALA   A CA  1 
ATOM   1151 C C   . ALA   A 1 149 ? -9.608  13.016  4.728   1.00 29.72  ? 146 ALA   A C   1 
ATOM   1152 O O   . ALA   A 1 149 ? -9.953  13.042  3.540   1.00 28.02  ? 146 ALA   A O   1 
ATOM   1153 C CB  . ALA   A 1 149 ? -8.600  14.919  6.039   1.00 26.83  ? 146 ALA   A CB  1 
ATOM   1154 N N   . TRP   A 1 150 ? -9.010  11.953  5.270   1.00 29.14  ? 147 TRP   A N   1 
ATOM   1155 C CA  . TRP   A 1 150 ? -8.584  10.839  4.433   1.00 29.00  ? 147 TRP   A CA  1 
ATOM   1156 C C   . TRP   A 1 150 ? -9.773  10.060  3.881   1.00 30.72  ? 147 TRP   A C   1 
ATOM   1157 O O   . TRP   A 1 150 ? -9.766  9.651   2.707   1.00 27.17  ? 147 TRP   A O   1 
ATOM   1158 C CB  . TRP   A 1 150 ? -7.663  9.926   5.230   1.00 26.11  ? 147 TRP   A CB  1 
ATOM   1159 C CG  . TRP   A 1 150 ? -7.401  8.645   4.551   1.00 30.14  ? 147 TRP   A CG  1 
ATOM   1160 C CD1 . TRP   A 1 150 ? -6.419  8.385   3.638   1.00 28.00  ? 147 TRP   A CD1 1 
ATOM   1161 C CD2 . TRP   A 1 150 ? -8.140  7.430   4.709   1.00 28.79  ? 147 TRP   A CD2 1 
ATOM   1162 N NE1 . TRP   A 1 150 ? -6.492  7.074   3.231   1.00 34.98  ? 147 TRP   A NE1 1 
ATOM   1163 C CE2 . TRP   A 1 150 ? -7.543  6.468   3.870   1.00 31.53  ? 147 TRP   A CE2 1 
ATOM   1164 C CE3 . TRP   A 1 150 ? -9.241  7.059   5.488   1.00 29.51  ? 147 TRP   A CE3 1 
ATOM   1165 C CZ2 . TRP   A 1 150 ? -8.011  5.164   3.782   1.00 32.84  ? 147 TRP   A CZ2 1 
ATOM   1166 C CZ3 . TRP   A 1 150 ? -9.708  5.762   5.402   1.00 30.61  ? 147 TRP   A CZ3 1 
ATOM   1167 C CH2 . TRP   A 1 150 ? -9.092  4.828   4.551   1.00 30.30  ? 147 TRP   A CH2 1 
ATOM   1168 N N   . GLY   A 1 151 ? -10.790 9.824   4.719   1.00 26.63  ? 148 GLY   A N   1 
ATOM   1169 C CA  . GLY   A 1 151 ? -12.000 9.177   4.234   1.00 28.08  ? 148 GLY   A CA  1 
ATOM   1170 C C   . GLY   A 1 151 ? -12.683 9.965   3.127   1.00 32.20  ? 148 GLY   A C   1 
ATOM   1171 O O   . GLY   A 1 151 ? -13.079 9.398   2.105   1.00 30.21  ? 148 GLY   A O   1 
ATOM   1172 N N   . THR   A 1 152 ? -12.827 11.285  3.311   1.00 32.36  ? 149 THR   A N   1 
ATOM   1173 C CA  . THR   A 1 152 ? -13.487 12.106  2.295   1.00 30.42  ? 149 THR   A CA  1 
ATOM   1174 C C   . THR   A 1 152 ? -12.738 12.032  0.973   1.00 31.63  ? 149 THR   A C   1 
ATOM   1175 O O   . THR   A 1 152 ? -13.341 11.795  -0.080  1.00 31.19  ? 149 THR   A O   1 
ATOM   1176 C CB  . THR   A 1 152 ? -13.600 13.565  2.756   1.00 29.74  ? 149 THR   A CB  1 
ATOM   1177 O OG1 . THR   A 1 152 ? -14.385 13.652  3.964   1.00 27.49  ? 149 THR   A OG1 1 
ATOM   1178 C CG2 . THR   A 1 152 ? -14.272 14.387  1.664   1.00 28.20  ? 149 THR   A CG2 1 
ATOM   1179 N N   . MET   A 1 153 ? -11.408 12.175  1.020   1.00 27.46  ? 150 MET   A N   1 
ATOM   1180 C CA  . MET   A 1 153 ? -10.579 12.256  -0.174  1.00 29.64  ? 150 MET   A CA  1 
ATOM   1181 C C   . MET   A 1 153 ? -10.331 10.916  -0.857  1.00 31.74  ? 150 MET   A C   1 
ATOM   1182 O O   . MET   A 1 153 ? -9.737  10.905  -1.943  1.00 34.52  ? 150 MET   A O   1 
ATOM   1183 C CB  . MET   A 1 153 ? -9.238  12.899  0.171   1.00 26.90  ? 150 MET   A CB  1 
ATOM   1184 C CG  . MET   A 1 153 ? -9.393  14.225  0.837   1.00 29.62  ? 150 MET   A CG  1 
ATOM   1185 S SD  . MET   A 1 153 ? -10.348 15.340  -0.226  1.00 37.23  ? 150 MET   A SD  1 
ATOM   1186 C CE  . MET   A 1 153 ? -9.141  15.673  -1.501  1.00 23.81  ? 150 MET   A CE  1 
ATOM   1187 N N   . THR   A 1 154 ? -10.749 9.795   -0.264  1.00 27.62  ? 151 THR   A N   1 
ATOM   1188 C CA  . THR   A 1 154 ? -10.570 8.499   -0.892  1.00 26.42  ? 151 THR   A CA  1 
ATOM   1189 C C   . THR   A 1 154 ? -11.862 7.720   -1.065  1.00 32.78  ? 151 THR   A C   1 
ATOM   1190 O O   . THR   A 1 154 ? -11.886 6.782   -1.867  1.00 33.59  ? 151 THR   A O   1 
ATOM   1191 C CB  . THR   A 1 154 ? -9.580  7.632   -0.094  1.00 29.41  ? 151 THR   A CB  1 
ATOM   1192 O OG1 . THR   A 1 154 ? -10.085 7.379   1.232   1.00 31.08  ? 151 THR   A OG1 1 
ATOM   1193 C CG2 . THR   A 1 154 ? -8.228  8.322   -0.003  1.00 32.19  ? 151 THR   A CG2 1 
ATOM   1194 N N   . LYS   A 1 155 ? -12.925 8.073   -0.342  1.00 29.44  ? 152 LYS   A N   1 
ATOM   1195 C CA  . LYS   A 1 155 ? -14.213 7.406   -0.441  1.00 28.18  ? 152 LYS   A CA  1 
ATOM   1196 C C   . LYS   A 1 155 ? -15.283 8.253   -1.127  1.00 34.35  ? 152 LYS   A C   1 
ATOM   1197 O O   . LYS   A 1 155 ? -16.377 7.746   -1.395  1.00 39.88  ? 152 LYS   A O   1 
ATOM   1198 C CB  . LYS   A 1 155 ? -14.712 7.008   0.961   1.00 29.97  ? 152 LYS   A CB  1 
ATOM   1199 C CG  . LYS   A 1 155 ? -13.669 6.323   1.848   1.00 29.75  ? 152 LYS   A CG  1 
ATOM   1200 C CD  . LYS   A 1 155 ? -14.286 5.744   3.093   1.00 32.27  ? 152 LYS   A CD  1 
ATOM   1201 C CE  . LYS   A 1 155 ? -13.226 5.082   3.984   1.00 34.20  ? 152 LYS   A CE  1 
ATOM   1202 N NZ  . LYS   A 1 155 ? -12.648 3.842   3.414   1.00 33.96  ? 152 LYS   A NZ  1 
ATOM   1203 N N   . PHE   A 1 156 ? -15.022 9.524   -1.397  1.00 33.00  ? 153 PHE   A N   1 
ATOM   1204 C CA  . PHE   A 1 156 ? -16.046 10.347  -2.027  1.00 33.49  ? 153 PHE   A CA  1 
ATOM   1205 C C   . PHE   A 1 156 ? -15.435 11.239  -3.097  1.00 32.54  ? 153 PHE   A C   1 
ATOM   1206 O O   . PHE   A 1 156 ? -15.745 11.096  -4.283  1.00 33.72  ? 153 PHE   A O   1 
ATOM   1207 C CB  . PHE   A 1 156 ? -16.787 11.207  -0.993  1.00 28.51  ? 153 PHE   A CB  1 
ATOM   1208 C CG  . PHE   A 1 156 ? -17.571 12.325  -1.609  1.00 26.84  ? 153 PHE   A CG  1 
ATOM   1209 C CD1 . PHE   A 1 156 ? -18.589 12.060  -2.506  1.00 29.48  ? 153 PHE   A CD1 1 
ATOM   1210 C CD2 . PHE   A 1 156 ? -17.269 13.643  -1.328  1.00 28.73  ? 153 PHE   A CD2 1 
ATOM   1211 C CE1 . PHE   A 1 156 ? -19.304 13.094  -3.116  1.00 28.53  ? 153 PHE   A CE1 1 
ATOM   1212 C CE2 . PHE   A 1 156 ? -17.982 14.686  -1.919  1.00 29.64  ? 153 PHE   A CE2 1 
ATOM   1213 C CZ  . PHE   A 1 156 ? -19.008 14.404  -2.822  1.00 30.68  ? 153 PHE   A CZ  1 
ATOM   1214 N N   . MET   A 1 157 ? -14.588 12.175  -2.688  1.00 30.56  ? 154 MET   A N   1 
ATOM   1215 C CA  . MET   A 1 157 ? -13.972 13.078  -3.642  1.00 33.08  ? 154 MET   A CA  1 
ATOM   1216 C C   . MET   A 1 157 ? -12.958 12.354  -4.507  1.00 33.95  ? 154 MET   A C   1 
ATOM   1217 O O   . MET   A 1 157 ? -12.237 11.459  -4.050  1.00 39.30  ? 154 MET   A O   1 
ATOM   1218 C CB  . MET   A 1 157 ? -13.300 14.242  -2.929  1.00 33.97  ? 154 MET   A CB  1 
ATOM   1219 C CG  . MET   A 1 157 ? -14.070 15.523  -3.145  1.00 31.53  ? 154 MET   A CG  1 
ATOM   1220 S SD  . MET   A 1 157 ? -13.384 16.918  -2.269  1.00 47.09  ? 154 MET   A SD  1 
ATOM   1221 C CE  . MET   A 1 157 ? -14.893 17.827  -1.921  1.00 31.99  ? 154 MET   A CE  1 
ATOM   1222 N N   . GLN   A 1 158 ? -12.899 12.762  -5.761  1.00 30.43  ? 155 GLN   A N   1 
ATOM   1223 C CA  . GLN   A 1 158 ? -12.036 12.161  -6.777  1.00 36.31  ? 155 GLN   A CA  1 
ATOM   1224 C C   . GLN   A 1 158 ? -11.321 13.303  -7.462  1.00 35.26  ? 155 GLN   A C   1 
ATOM   1225 O O   . GLN   A 1 158 ? -11.669 13.660  -8.586  1.00 38.01  ? 155 GLN   A O   1 
ATOM   1226 C CB  . GLN   A 1 158 ? -12.843 11.333  -7.781  1.00 33.75  ? 155 GLN   A CB  1 
ATOM   1227 C CG  . GLN   A 1 158 ? -13.827 10.383  -7.127  1.00 39.97  ? 155 GLN   A CG  1 
ATOM   1228 C CD  . GLN   A 1 158 ? -14.670 9.601   -8.120  1.00 52.22  ? 155 GLN   A CD  1 
ATOM   1229 O OE1 . GLN   A 1 158 ? -15.650 10.115  -8.686  1.00 50.66  ? 155 GLN   A OE1 1 
ATOM   1230 N NE2 . GLN   A 1 158 ? -14.303 8.339   -8.324  1.00 54.35  ? 155 GLN   A NE2 1 
ATOM   1231 N N   . VAL   A 1 159 ? -10.345 13.894  -6.781  1.00 34.28  ? 156 VAL   A N   1 
ATOM   1232 C CA  . VAL   A 1 159 ? -9.568  14.965  -7.396  1.00 30.76  ? 156 VAL   A CA  1 
ATOM   1233 C C   . VAL   A 1 159 ? -8.740  14.394  -8.536  1.00 33.70  ? 156 VAL   A C   1 
ATOM   1234 O O   . VAL   A 1 159 ? -8.116  13.336  -8.400  1.00 37.84  ? 156 VAL   A O   1 
ATOM   1235 C CB  . VAL   A 1 159 ? -8.684  15.662  -6.353  1.00 29.18  ? 156 VAL   A CB  1 
ATOM   1236 C CG1 . VAL   A 1 159 ? -7.965  16.816  -6.983  1.00 31.26  ? 156 VAL   A CG1 1 
ATOM   1237 C CG2 . VAL   A 1 159 ? -9.535  16.170  -5.189  1.00 28.57  ? 156 VAL   A CG2 1 
ATOM   1238 N N   . ARG   A 1 160 ? -8.752  15.074  -9.661  1.00 32.51  ? 157 ARG   A N   1 
ATOM   1239 C CA  . ARG   A 1 160 ? -8.058  14.773  -10.892 1.00 32.62  ? 157 ARG   A CA  1 
ATOM   1240 C C   . ARG   A 1 160 ? -7.015  15.854  -11.183 1.00 36.63  ? 157 ARG   A C   1 
ATOM   1241 O O   . ARG   A 1 160 ? -7.210  17.016  -10.807 1.00 37.88  ? 157 ARG   A O   1 
ATOM   1242 C CB  . ARG   A 1 160 ? -9.050  14.710  -12.062 1.00 35.01  ? 157 ARG   A CB  1 
ATOM   1243 C CG  . ARG   A 1 160 ? -10.093 13.626  -11.977 1.00 34.29  ? 157 ARG   A CG  1 
ATOM   1244 C CD  . ARG   A 1 160 ? -9.462  12.287  -11.693 1.00 41.53  ? 157 ARG   A CD  1 
ATOM   1245 N NE  . ARG   A 1 160 ? -8.394  11.953  -12.633 1.00 45.85  ? 157 ARG   A NE  1 
ATOM   1246 C CZ  . ARG   A 1 160 ? -7.385  11.130  -12.355 1.00 50.26  ? 157 ARG   A CZ  1 
ATOM   1247 N NH1 . ARG   A 1 160 ? -7.274  10.547  -11.162 1.00 49.06  ? 157 ARG   A NH1 1 
ATOM   1248 N NH2 . ARG   A 1 160 ? -6.455  10.900  -13.288 1.00 40.41  ? 157 ARG   A NH2 1 
ATOM   1249 N N   . PRO   A 1 161 ? -5.913  15.526  -11.870 1.00 33.44  ? 158 PRO   A N   1 
ATOM   1250 C CA  . PRO   A 1 161 ? -4.911  16.562  -12.184 1.00 32.42  ? 158 PRO   A CA  1 
ATOM   1251 C C   . PRO   A 1 161 ? -5.525  17.677  -13.017 1.00 32.17  ? 158 PRO   A C   1 
ATOM   1252 O O   . PRO   A 1 161 ? -6.293  17.432  -13.947 1.00 31.10  ? 158 PRO   A O   1 
ATOM   1253 C CB  . PRO   A 1 161 ? -3.832  15.805  -12.966 1.00 32.08  ? 158 PRO   A CB  1 
ATOM   1254 C CG  . PRO   A 1 161 ? -4.078  14.352  -12.682 1.00 36.68  ? 158 PRO   A CG  1 
ATOM   1255 C CD  . PRO   A 1 161 ? -5.539  14.201  -12.395 1.00 35.74  ? 158 PRO   A CD  1 
ATOM   1256 N N   . GLY   A 1 162 ? -5.179  18.912  -12.680 1.00 28.24  ? 159 GLY   A N   1 
ATOM   1257 C CA  . GLY   A 1 162 ? -5.787  20.043  -13.339 1.00 30.70  ? 159 GLY   A CA  1 
ATOM   1258 C C   . GLY   A 1 162 ? -7.029  20.599  -12.668 1.00 38.32  ? 159 GLY   A C   1 
ATOM   1259 O O   . GLY   A 1 162 ? -7.444  21.708  -13.014 1.00 34.16  ? 159 GLY   A O   1 
ATOM   1260 N N   . ASP   A 1 163 ? -7.627  19.880  -11.710 1.00 35.09  ? 160 ASP   A N   1 
ATOM   1261 C CA  . ASP   A 1 163 ? -8.788  20.398  -10.993 1.00 33.54  ? 160 ASP   A CA  1 
ATOM   1262 C C   . ASP   A 1 163 ? -8.429  21.599  -10.122 1.00 32.83  ? 160 ASP   A C   1 
ATOM   1263 O O   . ASP   A 1 163 ? -7.304  21.725  -9.625  1.00 33.64  ? 160 ASP   A O   1 
ATOM   1264 C CB  . ASP   A 1 163 ? -9.392  19.318  -10.095 1.00 32.28  ? 160 ASP   A CB  1 
ATOM   1265 C CG  . ASP   A 1 163 ? -10.290 18.361  -10.846 1.00 35.45  ? 160 ASP   A CG  1 
ATOM   1266 O OD1 . ASP   A 1 163 ? -10.635 18.617  -12.032 1.00 36.88  ? 160 ASP   A OD1 1 
ATOM   1267 O OD2 . ASP   A 1 163 ? -10.657 17.345  -10.224 1.00 34.44  ? 160 ASP   A OD2 1 
ATOM   1268 N N   . THR   A 1 164 ? -9.411  22.474  -9.917  1.00 26.62  ? 161 THR   A N   1 
ATOM   1269 C CA  . THR   A 1 164 ? -9.339  23.499  -8.883  1.00 29.80  ? 161 THR   A CA  1 
ATOM   1270 C C   . THR   A 1 164 ? -10.152 23.059  -7.664  1.00 31.34  ? 161 THR   A C   1 
ATOM   1271 O O   . THR   A 1 164 ? -11.353 22.769  -7.779  1.00 29.84  ? 161 THR   A O   1 
ATOM   1272 C CB  . THR   A 1 164 ? -9.847  24.847  -9.394  1.00 29.80  ? 161 THR   A CB  1 
ATOM   1273 O OG1 . THR   A 1 164 ? -9.002  25.309  -10.470 1.00 33.05  ? 161 THR   A OG1 1 
ATOM   1274 C CG2 . THR   A 1 164 ? -9.829  25.867  -8.256  1.00 25.63  ? 161 THR   A CG2 1 
ATOM   1275 N N   . VAL   A 1 165 ? -9.499  23.012  -6.501  1.00 30.13  ? 162 VAL   A N   1 
ATOM   1276 C CA  . VAL   A 1 165 ? -10.131 22.605  -5.249  1.00 27.54  ? 162 VAL   A CA  1 
ATOM   1277 C C   . VAL   A 1 165 ? -10.152 23.804  -4.323  1.00 29.15  ? 162 VAL   A C   1 
ATOM   1278 O O   . VAL   A 1 165 ? -9.128  24.475  -4.142  1.00 30.47  ? 162 VAL   A O   1 
ATOM   1279 C CB  . VAL   A 1 165 ? -9.402  21.427  -4.574  1.00 27.00  ? 162 VAL   A CB  1 
ATOM   1280 C CG1 . VAL   A 1 165 ? -10.161 21.017  -3.335  1.00 24.44  ? 162 VAL   A CG1 1 
ATOM   1281 C CG2 . VAL   A 1 165 ? -9.274  20.249  -5.512  1.00 23.34  ? 162 VAL   A CG2 1 
ATOM   1282 N N   . VAL   A 1 166 ? -11.317 24.081  -3.748  1.00 26.90  ? 163 VAL   A N   1 
ATOM   1283 C CA  . VAL   A 1 166 ? -11.477 25.143  -2.769  1.00 28.59  ? 163 VAL   A CA  1 
ATOM   1284 C C   . VAL   A 1 166 ? -11.701 24.467  -1.429  1.00 30.40  ? 163 VAL   A C   1 
ATOM   1285 O O   . VAL   A 1 166 ? -12.452 23.488  -1.343  1.00 30.14  ? 163 VAL   A O   1 
ATOM   1286 C CB  . VAL   A 1 166 ? -12.640 26.097  -3.120  1.00 28.43  ? 163 VAL   A CB  1 
ATOM   1287 C CG1 . VAL   A 1 166 ? -12.933 27.050  -1.965  1.00 28.84  ? 163 VAL   A CG1 1 
ATOM   1288 C CG2 . VAL   A 1 166 ? -12.341 26.898  -4.361  1.00 27.82  ? 163 VAL   A CG2 1 
ATOM   1289 N N   . VAL   A 1 167 ? -11.025 24.966  -0.395  1.00 28.18  ? 164 VAL   A N   1 
ATOM   1290 C CA  . VAL   A 1 167 ? -11.143 24.458  0.970   1.00 28.38  ? 164 VAL   A CA  1 
ATOM   1291 C C   . VAL   A 1 167 ? -11.405 25.663  1.852   1.00 31.84  ? 164 VAL   A C   1 
ATOM   1292 O O   . VAL   A 1 167 ? -10.513 26.506  2.022   1.00 32.38  ? 164 VAL   A O   1 
ATOM   1293 C CB  . VAL   A 1 167 ? -9.878  23.713  1.443   1.00 31.21  ? 164 VAL   A CB  1 
ATOM   1294 C CG1 . VAL   A 1 167 ? -10.081 23.109  2.828   1.00 29.75  ? 164 VAL   A CG1 1 
ATOM   1295 C CG2 . VAL   A 1 167 ? -9.466  22.632  0.462   1.00 24.52  ? 164 VAL   A CG2 1 
ATOM   1296 N N   . SER   A 1 168 ? -12.621 25.756  2.407   1.00 31.87  ? 165 SER   A N   1 
ATOM   1297 C CA  . SER   A 1 168 ? -12.925 26.745  3.436   1.00 32.99  ? 165 SER   A CA  1 
ATOM   1298 C C   . SER   A 1 168 ? -12.553 26.215  4.823   1.00 37.79  ? 165 SER   A C   1 
ATOM   1299 O O   . SER   A 1 168 ? -12.563 25.005  5.072   1.00 40.09  ? 165 SER   A O   1 
ATOM   1300 C CB  . SER   A 1 168 ? -14.402 27.131  3.399   1.00 31.58  ? 165 SER   A CB  1 
ATOM   1301 O OG  . SER   A 1 168 ? -15.225 26.017  3.652   1.00 36.65  ? 165 SER   A OG  1 
ATOM   1302 N N   . GLY   A 1 169 ? -12.221 27.129  5.731   1.00 38.74  ? 166 GLY   A N   1 
ATOM   1303 C CA  . GLY   A 1 169 ? -11.702 26.700  7.018   1.00 37.50  ? 166 GLY   A CA  1 
ATOM   1304 C C   . GLY   A 1 169 ? -10.378 25.989  6.870   1.00 40.15  ? 166 GLY   A C   1 
ATOM   1305 O O   . GLY   A 1 169 ? -10.133 24.968  7.528   1.00 40.03  ? 166 GLY   A O   1 
ATOM   1306 N N   . ALA   A 1 170 ? -9.513  26.512  6.007   1.00 40.95  ? 167 ALA   A N   1 
ATOM   1307 C CA  . ALA   A 1 170 ? -8.358  25.762  5.550   1.00 37.45  ? 167 ALA   A CA  1 
ATOM   1308 C C   . ALA   A 1 170 ? -7.221  25.705  6.567   1.00 39.98  ? 167 ALA   A C   1 
ATOM   1309 O O   . ALA   A 1 170 ? -6.420  24.774  6.512   1.00 41.04  ? 167 ALA   A O   1 
ATOM   1310 C CB  . ALA   A 1 170 ? -7.868  26.347  4.229   1.00 29.15  ? 167 ALA   A CB  1 
ATOM   1311 N N   . SER   A 1 171 ? -7.134  26.637  7.511   1.00 44.05  ? 168 SER   A N   1 
ATOM   1312 C CA  . SER   A 1 171 ? -5.953  26.670  8.371   1.00 44.24  ? 168 SER   A CA  1 
ATOM   1313 C C   . SER   A 1 171 ? -5.928  25.572  9.432   1.00 39.29  ? 168 SER   A C   1 
ATOM   1314 O O   . SER   A 1 171 ? -4.843  25.231  9.911   1.00 46.44  ? 168 SER   A O   1 
ATOM   1315 C CB  . SER   A 1 171 ? -5.839  28.031  9.051   1.00 45.76  ? 168 SER   A CB  1 
ATOM   1316 O OG  . SER   A 1 171 ? -7.032  28.298  9.749   1.00 53.55  ? 168 SER   A OG  1 
ATOM   1317 N N   . GLY   A 1 172 ? -7.078  25.020  9.814   1.00 40.94  ? 169 GLY   A N   1 
ATOM   1318 C CA  . GLY   A 1 172 ? -7.125  23.922  10.756  1.00 36.32  ? 169 GLY   A CA  1 
ATOM   1319 C C   . GLY   A 1 172 ? -6.549  22.636  10.176  1.00 44.14  ? 169 GLY   A C   1 
ATOM   1320 O O   . GLY   A 1 172 ? -6.110  22.554  9.022   1.00 40.99  ? 169 GLY   A O   1 
ATOM   1321 N N   . MET   A 1 173 ? -6.562  21.593  11.006  1.00 40.68  ? 170 MET   A N   1 
ATOM   1322 C CA  . MET   A 1 173 ? -5.873  20.375  10.597  1.00 39.46  ? 170 MET   A CA  1 
ATOM   1323 C C   . MET   A 1 173 ? -6.596  19.683  9.444   1.00 38.33  ? 170 MET   A C   1 
ATOM   1324 O O   . MET   A 1 173 ? -5.953  19.188  8.505   1.00 32.52  ? 170 MET   A O   1 
ATOM   1325 C CB  . MET   A 1 173 ? -5.715  19.403  11.764  1.00 37.20  ? 170 MET   A CB  1 
ATOM   1326 C CG  . MET   A 1 173 ? -5.503  17.991  11.229  1.00 39.55  ? 170 MET   A CG  1 
ATOM   1327 S SD  . MET   A 1 173 ? -4.737  16.772  12.260  1.00 43.63  ? 170 MET   A SD  1 
ATOM   1328 C CE  . MET   A 1 173 ? -3.151  17.527  12.612  1.00 40.99  ? 170 MET   A CE  1 
ATOM   1329 N N   . ILE   A 1 174 ? -7.929  19.603  9.520   1.00 38.63  ? 171 ILE   A N   1 
ATOM   1330 C CA  . ILE   A 1 174 ? -8.697  18.909  8.490   1.00 33.95  ? 171 ILE   A CA  1 
ATOM   1331 C C   . ILE   A 1 174 ? -8.572  19.638  7.158   1.00 34.12  ? 171 ILE   A C   1 
ATOM   1332 O O   . ILE   A 1 174 ? -8.346  19.012  6.108   1.00 32.01  ? 171 ILE   A O   1 
ATOM   1333 C CB  . ILE   A 1 174 ? -10.164 18.760  8.930   1.00 32.14  ? 171 ILE   A CB  1 
ATOM   1334 C CG1 . ILE   A 1 174 ? -10.265 17.887  10.180  1.00 32.59  ? 171 ILE   A CG1 1 
ATOM   1335 C CG2 . ILE   A 1 174 ? -10.996 18.125  7.847   1.00 30.16  ? 171 ILE   A CG2 1 
ATOM   1336 C CD1 . ILE   A 1 174 ? -11.715 17.596  10.626  1.00 31.02  ? 171 ILE   A CD1 1 
ATOM   1337 N N   . GLY   A 1 175 ? -8.675  20.970  7.183   1.00 33.93  ? 172 GLY   A N   1 
ATOM   1338 C CA  . GLY   A 1 175 ? -8.486  21.744  5.964   1.00 38.65  ? 172 GLY   A CA  1 
ATOM   1339 C C   . GLY   A 1 175 ? -7.114  21.557  5.333   1.00 35.49  ? 172 GLY   A C   1 
ATOM   1340 O O   . GLY   A 1 175 ? -6.998  21.360  4.116   1.00 32.02  ? 172 GLY   A O   1 
ATOM   1341 N N   . THR   A 1 176 ? -6.053  21.618  6.148   1.00 35.50  ? 173 THR   A N   1 
ATOM   1342 C CA  . THR   A 1 176 ? -4.708  21.514  5.586   1.00 33.91  ? 173 THR   A CA  1 
ATOM   1343 C C   . THR   A 1 176 ? -4.435  20.111  5.062   1.00 33.96  ? 173 THR   A C   1 
ATOM   1344 O O   . THR   A 1 176 ? -3.708  19.940  4.074   1.00 32.35  ? 173 THR   A O   1 
ATOM   1345 C CB  . THR   A 1 176 ? -3.642  21.887  6.622   1.00 35.87  ? 173 THR   A CB  1 
ATOM   1346 O OG1 . THR   A 1 176 ? -3.728  20.987  7.722   1.00 38.55  ? 173 THR   A OG1 1 
ATOM   1347 C CG2 . THR   A 1 176 ? -3.816  23.317  7.111   1.00 34.50  ? 173 THR   A CG2 1 
ATOM   1348 N N   . LEU   A 1 177 ? -4.992  19.088  5.714   1.00 32.98  ? 174 LEU   A N   1 
ATOM   1349 C CA  . LEU   A 1 177 ? -4.848  17.738  5.182   1.00 31.29  ? 174 LEU   A CA  1 
ATOM   1350 C C   . LEU   A 1 177 ? -5.532  17.614  3.819   1.00 32.65  ? 174 LEU   A C   1 
ATOM   1351 O O   . LEU   A 1 177 ? -4.943  17.109  2.857   1.00 31.02  ? 174 LEU   A O   1 
ATOM   1352 C CB  . LEU   A 1 177 ? -5.411  16.732  6.174   1.00 30.37  ? 174 LEU   A CB  1 
ATOM   1353 C CG  . LEU   A 1 177 ? -4.556  16.459  7.406   1.00 34.75  ? 174 LEU   A CG  1 
ATOM   1354 C CD1 . LEU   A 1 177 ? -5.289  15.562  8.407   1.00 33.25  ? 174 LEU   A CD1 1 
ATOM   1355 C CD2 . LEU   A 1 177 ? -3.251  15.820  6.967   1.00 34.47  ? 174 LEU   A CD2 1 
ATOM   1356 N N   . VAL   A 1 178 ? -6.769  18.102  3.713   1.00 29.46  ? 175 VAL   A N   1 
ATOM   1357 C CA  . VAL   A 1 178 ? -7.497  18.009  2.452   1.00 33.49  ? 175 VAL   A CA  1 
ATOM   1358 C C   . VAL   A 1 178 ? -6.745  18.726  1.342   1.00 32.15  ? 175 VAL   A C   1 
ATOM   1359 O O   . VAL   A 1 178 ? -6.648  18.225  0.214   1.00 32.04  ? 175 VAL   A O   1 
ATOM   1360 C CB  . VAL   A 1 178 ? -8.927  18.563  2.598   1.00 33.91  ? 175 VAL   A CB  1 
ATOM   1361 C CG1 . VAL   A 1 178 ? -9.531  18.761  1.213   1.00 28.85  ? 175 VAL   A CG1 1 
ATOM   1362 C CG2 . VAL   A 1 178 ? -9.793  17.614  3.447   1.00 30.22  ? 175 VAL   A CG2 1 
ATOM   1363 N N   . GLY   A 1 179 ? -6.209  19.911  1.633   1.00 33.23  ? 176 GLY   A N   1 
ATOM   1364 C CA  . GLY   A 1 179 ? -5.498  20.647  0.601   1.00 25.96  ? 176 GLY   A CA  1 
ATOM   1365 C C   . GLY   A 1 179 ? -4.231  19.940  0.160   1.00 32.69  ? 176 GLY   A C   1 
ATOM   1366 O O   . GLY   A 1 179 ? -3.908  19.907  -1.034  1.00 30.70  ? 176 GLY   A O   1 
ATOM   1367 N N   . GLN   A 1 180 ? -3.494  19.366  1.114   1.00 29.90  ? 177 GLN   A N   1 
ATOM   1368 C CA  . GLN   A 1 180 ? -2.248  18.702  0.765   1.00 27.52  ? 177 GLN   A CA  1 
ATOM   1369 C C   . GLN   A 1 180 ? -2.502  17.435  -0.034  1.00 26.17  ? 177 GLN   A C   1 
ATOM   1370 O O   . GLN   A 1 180 ? -1.743  17.121  -0.954  1.00 33.22  ? 177 GLN   A O   1 
ATOM   1371 C CB  . GLN   A 1 180 ? -1.451  18.387  2.024   1.00 29.97  ? 177 GLN   A CB  1 
ATOM   1372 C CG  . GLN   A 1 180 ? -0.952  19.608  2.722   1.00 32.16  ? 177 GLN   A CG  1 
ATOM   1373 C CD  . GLN   A 1 180 ? -0.289  19.278  4.038   1.00 37.93  ? 177 GLN   A CD  1 
ATOM   1374 O OE1 . GLN   A 1 180 ? 0.877   18.884  4.075   1.00 38.90  ? 177 GLN   A OE1 1 
ATOM   1375 N NE2 . GLN   A 1 180 ? -1.033  19.420  5.129   1.00 34.71  ? 177 GLN   A NE2 1 
ATOM   1376 N N   . MET   A 1 181 ? -3.552  16.685  0.309   1.00 32.21  ? 178 MET   A N   1 
ATOM   1377 C CA  . MET   A 1 181 ? -3.935  15.523  -0.493  1.00 30.41  ? 178 MET   A CA  1 
ATOM   1378 C C   . MET   A 1 181 ? -4.390  15.944  -1.886  1.00 28.92  ? 178 MET   A C   1 
ATOM   1379 O O   . MET   A 1 181 ? -3.995  15.336  -2.886  1.00 28.08  ? 178 MET   A O   1 
ATOM   1380 C CB  . MET   A 1 181 ? -5.038  14.733  0.216   1.00 26.27  ? 178 MET   A CB  1 
ATOM   1381 C CG  . MET   A 1 181 ? -4.696  14.373  1.649   1.00 30.75  ? 178 MET   A CG  1 
ATOM   1382 S SD  . MET   A 1 181 ? -5.924  13.336  2.481   1.00 35.82  ? 178 MET   A SD  1 
ATOM   1383 C CE  . MET   A 1 181 ? -5.443  11.744  1.777   1.00 45.98  ? 178 MET   A CE  1 
ATOM   1384 N N   . ALA   A 1 182 ? -5.221  16.987  -1.966  1.00 26.28  ? 179 ALA   A N   1 
ATOM   1385 C CA  . ALA   A 1 182 ? -5.664  17.488  -3.258  1.00 28.96  ? 179 ALA   A CA  1 
ATOM   1386 C C   . ALA   A 1 182 ? -4.471  17.869  -4.116  1.00 28.95  ? 179 ALA   A C   1 
ATOM   1387 O O   . ALA   A 1 182 ? -4.429  17.575  -5.320  1.00 24.83  ? 179 ALA   A O   1 
ATOM   1388 C CB  . ALA   A 1 182 ? -6.586  18.690  -3.058  1.00 26.32  ? 179 ALA   A CB  1 
ATOM   1389 N N   . LYS   A 1 183 ? -3.487  18.514  -3.500  1.00 28.33  ? 180 LYS   A N   1 
ATOM   1390 C CA  . LYS   A 1 183 ? -2.280  18.899  -4.214  1.00 30.49  ? 180 LYS   A CA  1 
ATOM   1391 C C   . LYS   A 1 183 ? -1.580  17.667  -4.771  1.00 33.96  ? 180 LYS   A C   1 
ATOM   1392 O O   . LYS   A 1 183 ? -1.214  17.625  -5.955  1.00 31.20  ? 180 LYS   A O   1 
ATOM   1393 C CB  . LYS   A 1 183 ? -1.364  19.676  -3.272  1.00 28.42  ? 180 LYS   A CB  1 
ATOM   1394 C CG  . LYS   A 1 183 ? -0.326  20.476  -3.980  1.00 39.20  ? 180 LYS   A CG  1 
ATOM   1395 C CD  . LYS   A 1 183 ? -0.813  21.896  -4.087  1.00 44.15  ? 180 LYS   A CD  1 
ATOM   1396 C CE  . LYS   A 1 183 ? -0.070  22.660  -5.172  1.00 39.37  ? 180 LYS   A CE  1 
ATOM   1397 N NZ  . LYS   A 1 183 ? -0.948  22.846  -6.349  1.00 48.20  ? 180 LYS   A NZ  1 
ATOM   1398 N N   . ARG   A 1 184 ? -1.436  16.628  -3.934  1.00 30.07  ? 181 ARG   A N   1 
ATOM   1399 C CA  . ARG   A 1 184 ? -0.819  15.387  -4.388  1.00 28.84  ? 181 ARG   A CA  1 
ATOM   1400 C C   . ARG   A 1 184 ? -1.570  14.810  -5.576  1.00 34.18  ? 181 ARG   A C   1 
ATOM   1401 O O   . ARG   A 1 184 ? -0.967  14.204  -6.471  1.00 34.01  ? 181 ARG   A O   1 
ATOM   1402 C CB  . ARG   A 1 184 ? -0.780  14.367  -3.254  1.00 27.29  ? 181 ARG   A CB  1 
ATOM   1403 C CG  . ARG   A 1 184 ? 0.202   14.676  -2.157  1.00 36.55  ? 181 ARG   A CG  1 
ATOM   1404 C CD  . ARG   A 1 184 ? 0.232   13.533  -1.145  1.00 41.00  ? 181 ARG   A CD  1 
ATOM   1405 N NE  . ARG   A 1 184 ? 0.142   12.218  -1.781  1.00 37.49  ? 181 ARG   A NE  1 
ATOM   1406 C CZ  . ARG   A 1 184 ? 1.181   11.531  -2.231  1.00 36.40  ? 181 ARG   A CZ  1 
ATOM   1407 N NH1 . ARG   A 1 184 ? 2.414   12.023  -2.180  1.00 39.14  ? 181 ARG   A NH1 1 
ATOM   1408 N NH2 . ARG   A 1 184 ? 0.979   10.324  -2.751  1.00 43.84  ? 181 ARG   A NH2 1 
ATOM   1409 N N   . ALA   A 1 185 ? -2.893  14.956  -5.587  1.00 30.65  ? 182 ALA   A N   1 
ATOM   1410 C CA  . ALA   A 1 185 ? -3.670  14.437  -6.692  1.00 28.46  ? 182 ALA   A CA  1 
ATOM   1411 C C   . ALA   A 1 185 ? -3.617  15.349  -7.910  1.00 34.07  ? 182 ALA   A C   1 
ATOM   1412 O O   . ALA   A 1 185 ? -4.282  15.055  -8.905  1.00 30.63  ? 182 ALA   A O   1 
ATOM   1413 C CB  . ALA   A 1 185 ? -5.109  14.225  -6.250  1.00 25.37  ? 182 ALA   A CB  1 
ATOM   1414 N N   . GLY   A 1 186 ? -2.877  16.454  -7.838  1.00 28.66  ? 183 GLY   A N   1 
ATOM   1415 C CA  . GLY   A 1 186 ? -2.596  17.260  -8.999  1.00 33.68  ? 183 GLY   A CA  1 
ATOM   1416 C C   . GLY   A 1 186 ? -3.433  18.508  -9.174  1.00 36.37  ? 183 GLY   A C   1 
ATOM   1417 O O   . GLY   A 1 186 ? -3.496  19.035  -10.301 1.00 34.87  ? 183 GLY   A O   1 
ATOM   1418 N N   . ALA   A 1 187 ? -4.034  19.021  -8.103  1.00 29.33  ? 184 ALA   A N   1 
ATOM   1419 C CA  . ALA   A 1 187 ? -5.007  20.093  -8.184  1.00 27.32  ? 184 ALA   A CA  1 
ATOM   1420 C C   . ALA   A 1 187 ? -4.392  21.447  -7.878  1.00 30.08  ? 184 ALA   A C   1 
ATOM   1421 O O   . ALA   A 1 187 ? -3.434  21.561  -7.112  1.00 37.78  ? 184 ALA   A O   1 
ATOM   1422 C CB  . ALA   A 1 187 ? -6.157  19.836  -7.213  1.00 31.25  ? 184 ALA   A CB  1 
ATOM   1423 N N   . ARG   A 1 188 ? -4.947  22.479  -8.506  1.00 32.90  ? 185 ARG   A N   1 
ATOM   1424 C CA  . ARG   A 1 188 ? -4.850  23.816  -7.945  1.00 31.68  ? 185 ARG   A CA  1 
ATOM   1425 C C   . ARG   A 1 188 ? -5.717  23.873  -6.689  1.00 30.05  ? 185 ARG   A C   1 
ATOM   1426 O O   . ARG   A 1 188 ? -6.847  23.364  -6.669  1.00 26.72  ? 185 ARG   A O   1 
ATOM   1427 C CB  . ARG   A 1 188 ? -5.295  24.872  -8.966  1.00 26.35  ? 185 ARG   A CB  1 
ATOM   1428 C CG  . ARG   A 1 188 ? -5.172  26.306  -8.434  1.00 27.26  ? 185 ARG   A CG  1 
ATOM   1429 C CD  . ARG   A 1 188 ? -5.592  27.333  -9.450  1.00 24.68  ? 185 ARG   A CD  1 
ATOM   1430 N NE  . ARG   A 1 188 ? -5.651  28.699  -8.924  1.00 29.04  ? 185 ARG   A NE  1 
ATOM   1431 C CZ  . ARG   A 1 188 ? -4.600  29.487  -8.702  1.00 37.10  ? 185 ARG   A CZ  1 
ATOM   1432 N NH1 . ARG   A 1 188 ? -3.357  29.045  -8.827  1.00 35.21  ? 185 ARG   A NH1 1 
ATOM   1433 N NH2 . ARG   A 1 188 ? -4.799  30.752  -8.334  1.00 36.94  ? 185 ARG   A NH2 1 
ATOM   1434 N N   . VAL   A 1 189 ? -5.184  24.482  -5.636  1.00 29.63  ? 186 VAL   A N   1 
ATOM   1435 C CA  . VAL   A 1 189 ? -5.795  24.440  -4.311  1.00 31.55  ? 186 VAL   A CA  1 
ATOM   1436 C C   . VAL   A 1 189 ? -5.941  25.863  -3.790  1.00 31.91  ? 186 VAL   A C   1 
ATOM   1437 O O   . VAL   A 1 189 ? -4.940  26.565  -3.599  1.00 32.90  ? 186 VAL   A O   1 
ATOM   1438 C CB  . VAL   A 1 189 ? -4.967  23.594  -3.323  1.00 34.40  ? 186 VAL   A CB  1 
ATOM   1439 C CG1 . VAL   A 1 189 ? -5.636  23.545  -1.969  1.00 28.18  ? 186 VAL   A CG1 1 
ATOM   1440 C CG2 . VAL   A 1 189 ? -4.718  22.193  -3.879  1.00 29.60  ? 186 VAL   A CG2 1 
ATOM   1441 N N   . VAL   A 1 190 ? -7.182  26.278  -3.548  1.00 29.43  ? 187 VAL   A N   1 
ATOM   1442 C CA  . VAL   A 1 190 ? -7.503  27.593  -3.012  1.00 29.49  ? 187 VAL   A CA  1 
ATOM   1443 C C   . VAL   A 1 190 ? -8.025  27.411  -1.595  1.00 31.82  ? 187 VAL   A C   1 
ATOM   1444 O O   . VAL   A 1 190 ? -8.888  26.558  -1.352  1.00 33.29  ? 187 VAL   A O   1 
ATOM   1445 C CB  . VAL   A 1 190 ? -8.536  28.313  -3.894  1.00 29.91  ? 187 VAL   A CB  1 
ATOM   1446 C CG1 . VAL   A 1 190 ? -8.864  29.684  -3.319  1.00 28.64  ? 187 VAL   A CG1 1 
ATOM   1447 C CG2 . VAL   A 1 190 ? -8.013  28.417  -5.328  1.00 28.94  ? 187 VAL   A CG2 1 
ATOM   1448 N N   . GLY   A 1 191 ? -7.498  28.196  -0.661  1.00 32.44  ? 188 GLY   A N   1 
ATOM   1449 C CA  . GLY   A 1 191 ? -7.991  28.144  0.699   1.00 32.64  ? 188 GLY   A CA  1 
ATOM   1450 C C   . GLY   A 1 191 ? -8.457  29.482  1.256   1.00 37.47  ? 188 GLY   A C   1 
ATOM   1451 O O   . GLY   A 1 191 ? -8.174  30.553  0.712   1.00 35.85  ? 188 GLY   A O   1 
ATOM   1452 N N   . THR   A 1 192 ? -9.180  29.429  2.359   1.00 39.46  ? 189 THR   A N   1 
ATOM   1453 C CA  . THR   A 1 192 ? -9.522  30.615  3.118   1.00 42.60  ? 189 THR   A CA  1 
ATOM   1454 C C   . THR   A 1 192 ? -8.783  30.590  4.448   1.00 44.38  ? 189 THR   A C   1 
ATOM   1455 O O   . THR   A 1 192 ? -8.631  29.530  5.063   1.00 44.84  ? 189 THR   A O   1 
ATOM   1456 C CB  . THR   A 1 192 ? -11.026 30.702  3.343   1.00 45.00  ? 189 THR   A CB  1 
ATOM   1457 O OG1 . THR   A 1 192 ? -11.450 29.608  4.169   1.00 44.90  ? 189 THR   A OG1 1 
ATOM   1458 C CG2 . THR   A 1 192 ? -11.740 30.651  1.991   1.00 38.63  ? 189 THR   A CG2 1 
ATOM   1459 N N   . ALA   A 1 193 ? -8.295  31.757  4.865   1.00 44.92  ? 190 ALA   A N   1 
ATOM   1460 C CA  . ALA   A 1 193 ? -7.603  31.911  6.133   1.00 47.11  ? 190 ALA   A CA  1 
ATOM   1461 C C   . ALA   A 1 193 ? -7.969  33.265  6.721   1.00 53.29  ? 190 ALA   A C   1 
ATOM   1462 O O   . ALA   A 1 193 ? -8.549  34.122  6.051   1.00 51.84  ? 190 ALA   A O   1 
ATOM   1463 C CB  . ALA   A 1 193 ? -6.083  31.777  5.971   1.00 43.80  ? 190 ALA   A CB  1 
ATOM   1464 N N   . GLY   A 1 194 ? -7.623  33.455  7.989   1.00 58.81  ? 191 GLY   A N   1 
ATOM   1465 C CA  . GLY   A 1 194 ? -7.941  34.675  8.701   1.00 59.51  ? 191 GLY   A CA  1 
ATOM   1466 C C   . GLY   A 1 194 ? -6.800  35.646  8.888   1.00 56.04  ? 191 GLY   A C   1 
ATOM   1467 O O   . GLY   A 1 194 ? -6.994  36.675  9.545   1.00 60.80  ? 191 GLY   A O   1 
ATOM   1468 N N   . SER   A 1 195 ? -5.624  35.372  8.336   1.00 52.29  ? 192 SER   A N   1 
ATOM   1469 C CA  . SER   A 1 195 ? -4.489  36.225  8.648   1.00 60.21  ? 192 SER   A CA  1 
ATOM   1470 C C   . SER   A 1 195 ? -3.381  36.033  7.629   1.00 57.63  ? 192 SER   A C   1 
ATOM   1471 O O   . SER   A 1 195 ? -3.196  34.940  7.086   1.00 56.53  ? 192 SER   A O   1 
ATOM   1472 C CB  . SER   A 1 195 ? -3.956  35.936  10.049  1.00 61.01  ? 192 SER   A CB  1 
ATOM   1473 O OG  . SER   A 1 195 ? -3.307  37.079  10.560  1.00 72.19  ? 192 SER   A OG  1 
ATOM   1474 N N   . ALA   A 1 196 ? -2.629  37.113  7.404   1.00 58.90  ? 193 ALA   A N   1 
ATOM   1475 C CA  . ALA   A 1 196 ? -1.519  37.071  6.458   1.00 56.41  ? 193 ALA   A CA  1 
ATOM   1476 C C   . ALA   A 1 196 ? -0.510  35.992  6.829   1.00 58.14  ? 193 ALA   A C   1 
ATOM   1477 O O   . ALA   A 1 196 ? 0.076   35.351  5.949   1.00 53.29  ? 193 ALA   A O   1 
ATOM   1478 C CB  . ALA   A 1 196 ? -0.838  38.436  6.394   1.00 54.42  ? 193 ALA   A CB  1 
ATOM   1479 N N   . GLY   A 1 197 ? -0.280  35.788  8.126   1.00 61.28  ? 194 GLY   A N   1 
ATOM   1480 C CA  . GLY   A 1 197 ? 0.617   34.721  8.533   1.00 64.44  ? 194 GLY   A CA  1 
ATOM   1481 C C   . GLY   A 1 197 ? 0.016   33.351  8.287   1.00 60.17  ? 194 GLY   A C   1 
ATOM   1482 O O   . GLY   A 1 197 ? 0.671   32.461  7.731   1.00 58.87  ? 194 GLY   A O   1 
ATOM   1483 N N   . LYS   A 1 198 ? -1.244  33.168  8.696   1.00 55.79  ? 195 LYS   A N   1 
ATOM   1484 C CA  . LYS   A 1 198 ? -1.938  31.917  8.418   1.00 54.79  ? 195 LYS   A CA  1 
ATOM   1485 C C   . LYS   A 1 198 ? -2.034  31.675  6.919   1.00 53.51  ? 195 LYS   A C   1 
ATOM   1486 O O   . LYS   A 1 198 ? -1.886  30.539  6.453   1.00 49.81  ? 195 LYS   A O   1 
ATOM   1487 C CB  . LYS   A 1 198 ? -3.324  31.936  9.065   1.00 51.99  ? 195 LYS   A CB  1 
ATOM   1488 C CG  . LYS   A 1 198 ? -3.266  31.815  10.581  1.00 64.27  ? 195 LYS   A CG  1 
ATOM   1489 C CD  . LYS   A 1 198 ? -4.624  31.962  11.232  1.00 64.61  ? 195 LYS   A CD  1 
ATOM   1490 C CE  . LYS   A 1 198 ? -4.763  33.288  11.984  1.00 66.35  ? 195 LYS   A CE  1 
ATOM   1491 N NZ  . LYS   A 1 198 ? -6.172  33.789  12.124  1.00 59.79  ? 195 LYS   A NZ  1 
ATOM   1492 N N   . ALA   A 1 199 ? -2.270  32.737  6.149   1.00 51.20  ? 196 ALA   A N   1 
ATOM   1493 C CA  . ALA   A 1 199 ? -2.278  32.607  4.699   1.00 49.12  ? 196 ALA   A CA  1 
ATOM   1494 C C   . ALA   A 1 199 ? -0.898  32.231  4.167   1.00 51.41  ? 196 ALA   A C   1 
ATOM   1495 O O   . ALA   A 1 199 ? -0.785  31.436  3.219   1.00 48.22  ? 196 ALA   A O   1 
ATOM   1496 C CB  . ALA   A 1 199 ? -2.766  33.909  4.071   1.00 44.59  ? 196 ALA   A CB  1 
ATOM   1497 N N   . ARG   A 1 200 ? 0.165   32.782  4.766   1.00 48.73  ? 197 ARG   A N   1 
ATOM   1498 C CA  . ARG   A 1 200 ? 1.509   32.400  4.342   1.00 52.42  ? 197 ARG   A CA  1 
ATOM   1499 C C   . ARG   A 1 200 ? 1.830   30.983  4.774   1.00 47.07  ? 197 ARG   A C   1 
ATOM   1500 O O   . ARG   A 1 200 ? 2.521   30.258  4.054   1.00 48.69  ? 197 ARG   A O   1 
ATOM   1501 C CB  . ARG   A 1 200 ? 2.555   33.378  4.893   1.00 54.92  ? 197 ARG   A CB  1 
ATOM   1502 C CG  . ARG   A 1 200 ? 2.569   34.740  4.202   1.00 51.23  ? 197 ARG   A CG  1 
ATOM   1503 C CD  . ARG   A 1 200 ? 2.838   34.587  2.704   1.00 56.55  ? 197 ARG   A CD  1 
ATOM   1504 N NE  . ARG   A 1 200 ? 4.265   34.507  2.415   1.00 62.65  ? 197 ARG   A NE  1 
ATOM   1505 C CZ  . ARG   A 1 200 ? 4.804   33.736  1.478   1.00 66.32  ? 197 ARG   A CZ  1 
ATOM   1506 N NH1 . ARG   A 1 200 ? 4.062   32.920  0.740   1.00 58.66  ? 197 ARG   A NH1 1 
ATOM   1507 N NH2 . ARG   A 1 200 ? 6.124   33.776  1.284   1.00 64.44  ? 197 ARG   A NH2 1 
ATOM   1508 N N   . TYR   A 1 201 ? 1.311   30.570  5.930   1.00 48.75  ? 198 TYR   A N   1 
ATOM   1509 C CA  . TYR   A 1 201 ? 1.512   29.208  6.404   1.00 50.85  ? 198 TYR   A CA  1 
ATOM   1510 C C   . TYR   A 1 201 ? 0.852   28.192  5.468   1.00 49.99  ? 198 TYR   A C   1 
ATOM   1511 O O   . TYR   A 1 201 ? 1.454   27.158  5.138   1.00 48.72  ? 198 TYR   A O   1 
ATOM   1512 C CB  . TYR   A 1 201 ? 0.988   29.110  7.840   1.00 54.15  ? 198 TYR   A CB  1 
ATOM   1513 C CG  . TYR   A 1 201 ? 0.692   27.714  8.345   1.00 52.91  ? 198 TYR   A CG  1 
ATOM   1514 C CD1 . TYR   A 1 201 ? 1.714   26.850  8.724   1.00 54.14  ? 198 TYR   A CD1 1 
ATOM   1515 C CD2 . TYR   A 1 201 ? -0.618  27.274  8.470   1.00 55.16  ? 198 TYR   A CD2 1 
ATOM   1516 C CE1 . TYR   A 1 201 ? 1.436   25.577  9.197   1.00 53.21  ? 198 TYR   A CE1 1 
ATOM   1517 C CE2 . TYR   A 1 201 ? -0.914  26.003  8.932   1.00 54.60  ? 198 TYR   A CE2 1 
ATOM   1518 C CZ  . TYR   A 1 201 ? 0.112   25.157  9.300   1.00 56.91  ? 198 TYR   A CZ  1 
ATOM   1519 O OH  . TYR   A 1 201 ? -0.210  23.894  9.764   1.00 51.79  ? 198 TYR   A OH  1 
ATOM   1520 N N   . LEU   A 1 202 ? -0.370  28.482  5.005   1.00 40.01  ? 199 LEU   A N   1 
ATOM   1521 C CA  . LEU   A 1 202 ? -1.010  27.633  3.999   1.00 44.74  ? 199 LEU   A CA  1 
ATOM   1522 C C   . LEU   A 1 202 ? -0.266  27.651  2.668   1.00 44.19  ? 199 LEU   A C   1 
ATOM   1523 O O   . LEU   A 1 202 ? -0.259  26.647  1.944   1.00 42.68  ? 199 LEU   A O   1 
ATOM   1524 C CB  . LEU   A 1 202 ? -2.458  28.068  3.791   1.00 42.65  ? 199 LEU   A CB  1 
ATOM   1525 C CG  . LEU   A 1 202 ? -3.331  27.884  5.027   1.00 38.10  ? 199 LEU   A CG  1 
ATOM   1526 C CD1 . LEU   A 1 202 ? -4.769  28.232  4.709   1.00 38.20  ? 199 LEU   A CD1 1 
ATOM   1527 C CD2 . LEU   A 1 202 ? -3.199  26.467  5.498   1.00 38.08  ? 199 LEU   A CD2 1 
ATOM   1528 N N   . SER   A 1 203 ? 0.353   28.776  2.316   1.00 48.37  ? 200 SER   A N   1 
ATOM   1529 C CA  . SER   A 1 203 ? 1.184   28.791  1.119   1.00 45.38  ? 200 SER   A CA  1 
ATOM   1530 C C   . SER   A 1 203 ? 2.410   27.892  1.278   1.00 45.95  ? 200 SER   A C   1 
ATOM   1531 O O   . SER   A 1 203 ? 2.843   27.250  0.309   1.00 39.34  ? 200 SER   A O   1 
ATOM   1532 C CB  . SER   A 1 203 ? 1.590   30.224  0.803   1.00 44.45  ? 200 SER   A CB  1 
ATOM   1533 O OG  . SER   A 1 203 ? 1.892   30.360  -0.566  1.00 48.14  ? 200 SER   A OG  1 
ATOM   1534 N N   . GLN   A 1 204 ? 2.956   27.798  2.496   1.00 48.50  ? 201 GLN   A N   1 
ATOM   1535 C CA  . GLN   A 1 204 ? 4.067   26.874  2.739   1.00 53.47  ? 201 GLN   A CA  1 
ATOM   1536 C C   . GLN   A 1 204 ? 3.620   25.420  2.628   1.00 44.91  ? 201 GLN   A C   1 
ATOM   1537 O O   . GLN   A 1 204 ? 4.363   24.582  2.114   1.00 40.40  ? 201 GLN   A O   1 
ATOM   1538 C CB  . GLN   A 1 204 ? 4.694   27.127  4.115   1.00 54.65  ? 201 GLN   A CB  1 
ATOM   1539 C CG  . GLN   A 1 204 ? 5.115   28.581  4.334   1.00 65.20  ? 201 GLN   A CG  1 
ATOM   1540 C CD  . GLN   A 1 204 ? 6.247   28.743  5.337   1.00 73.93  ? 201 GLN   A CD  1 
ATOM   1541 O OE1 . GLN   A 1 204 ? 7.116   29.610  5.164   1.00 69.07  ? 201 GLN   A OE1 1 
ATOM   1542 N NE2 . GLN   A 1 204 ? 6.241   27.920  6.394   1.00 68.31  ? 201 GLN   A NE2 1 
ATOM   1543 N N   . LEU   A 1 205 ? 2.416   25.096  3.118   1.00 43.58  ? 202 LEU   A N   1 
ATOM   1544 C CA  . LEU   A 1 205 ? 1.874   23.751  2.943   1.00 42.50  ? 202 LEU   A CA  1 
ATOM   1545 C C   . LEU   A 1 205 ? 1.476   23.463  1.500   1.00 48.38  ? 202 LEU   A C   1 
ATOM   1546 O O   . LEU   A 1 205 ? 1.083   22.331  1.196   1.00 49.91  ? 202 LEU   A O   1 
ATOM   1547 C CB  . LEU   A 1 205 ? 0.672   23.542  3.869   1.00 41.90  ? 202 LEU   A CB  1 
ATOM   1548 C CG  . LEU   A 1 205 ? 1.004   23.748  5.354   1.00 42.41  ? 202 LEU   A CG  1 
ATOM   1549 C CD1 . LEU   A 1 205 ? -0.235  23.677  6.213   1.00 43.95  ? 202 LEU   A CD1 1 
ATOM   1550 C CD2 . LEU   A 1 205 ? 2.015   22.732  5.819   1.00 33.27  ? 202 LEU   A CD2 1 
ATOM   1551 N N   . GLY   A 1 206 ? 1.564   24.448  0.607   1.00 47.99  ? 203 GLY   A N   1 
ATOM   1552 C CA  . GLY   A 1 206 ? 1.358   24.218  -0.806  1.00 43.01  ? 203 GLY   A CA  1 
ATOM   1553 C C   . GLY   A 1 206 ? 0.055   24.728  -1.384  1.00 41.30  ? 203 GLY   A C   1 
ATOM   1554 O O   . GLY   A 1 206 ? -0.231  24.429  -2.543  1.00 39.01  ? 203 GLY   A O   1 
ATOM   1555 N N   . PHE   A 1 207 ? -0.750  25.475  -0.627  1.00 38.62  ? 204 PHE   A N   1 
ATOM   1556 C CA  . PHE   A 1 207 ? -1.902  26.134  -1.231  1.00 34.23  ? 204 PHE   A CA  1 
ATOM   1557 C C   . PHE   A 1 207 ? -1.445  27.103  -2.320  1.00 36.24  ? 204 PHE   A C   1 
ATOM   1558 O O   . PHE   A 1 207 ? -0.451  27.814  -2.167  1.00 41.30  ? 204 PHE   A O   1 
ATOM   1559 C CB  . PHE   A 1 207 ? -2.711  26.866  -0.163  1.00 34.21  ? 204 PHE   A CB  1 
ATOM   1560 C CG  . PHE   A 1 207 ? -3.634  25.977  0.607   1.00 32.33  ? 204 PHE   A CG  1 
ATOM   1561 C CD1 . PHE   A 1 207 ? -3.139  24.951  1.392   1.00 35.94  ? 204 PHE   A CD1 1 
ATOM   1562 C CD2 . PHE   A 1 207 ? -5.003  26.160  0.547   1.00 37.86  ? 204 PHE   A CD2 1 
ATOM   1563 C CE1 . PHE   A 1 207 ? -3.998  24.118  2.112   1.00 33.73  ? 204 PHE   A CE1 1 
ATOM   1564 C CE2 . PHE   A 1 207 ? -5.870  25.327  1.253   1.00 35.89  ? 204 PHE   A CE2 1 
ATOM   1565 C CZ  . PHE   A 1 207 ? -5.358  24.308  2.042   1.00 34.35  ? 204 PHE   A CZ  1 
ATOM   1566 N N   . ASP   A 1 208 ? -2.155  27.118  -3.441  1.00 40.01  ? 205 ASP   A N   1 
ATOM   1567 C CA  . ASP   A 1 208 ? -1.752  27.984  -4.540  1.00 38.80  ? 205 ASP   A CA  1 
ATOM   1568 C C   . ASP   A 1 208 ? -2.287  29.396  -4.385  1.00 40.06  ? 205 ASP   A C   1 
ATOM   1569 O O   . ASP   A 1 208 ? -1.712  30.343  -4.941  1.00 40.19  ? 205 ASP   A O   1 
ATOM   1570 C CB  . ASP   A 1 208 ? -2.218  27.397  -5.868  1.00 37.85  ? 205 ASP   A CB  1 
ATOM   1571 C CG  . ASP   A 1 208 ? -1.600  26.052  -6.143  1.00 45.35  ? 205 ASP   A CG  1 
ATOM   1572 O OD1 . ASP   A 1 208 ? -0.447  25.982  -6.628  1.00 56.10  ? 205 ASP   A OD1 1 
ATOM   1573 O OD2 . ASP   A 1 208 ? -2.269  25.049  -5.847  1.00 47.61  ? 205 ASP   A OD2 1 
ATOM   1574 N N   . ALA   A 1 209 ? -3.373  29.553  -3.646  1.00 41.64  ? 206 ALA   A N   1 
ATOM   1575 C CA  . ALA   A 1 209 ? -3.961  30.857  -3.402  1.00 37.62  ? 206 ALA   A CA  1 
ATOM   1576 C C   . ALA   A 1 209 ? -4.731  30.749  -2.104  1.00 35.42  ? 206 ALA   A C   1 
ATOM   1577 O O   . ALA   A 1 209 ? -5.303  29.698  -1.806  1.00 36.33  ? 206 ALA   A O   1 
ATOM   1578 C CB  . ALA   A 1 209 ? -4.880  31.288  -4.550  1.00 36.54  ? 206 ALA   A CB  1 
ATOM   1579 N N   . VAL   A 1 210 ? -4.701  31.814  -1.316  1.00 35.47  ? 207 VAL   A N   1 
ATOM   1580 C CA  . VAL   A 1 210 ? -5.407  31.862  -0.048  1.00 35.69  ? 207 VAL   A CA  1 
ATOM   1581 C C   . VAL   A 1 210 ? -6.178  33.168  0.002   1.00 42.24  ? 207 VAL   A C   1 
ATOM   1582 O O   . VAL   A 1 210 ? -5.612  34.235  -0.250  1.00 46.45  ? 207 VAL   A O   1 
ATOM   1583 C CB  . VAL   A 1 210 ? -4.448  31.747  1.148   1.00 39.78  ? 207 VAL   A CB  1 
ATOM   1584 C CG1 . VAL   A 1 210 ? -5.246  31.517  2.432   1.00 41.74  ? 207 VAL   A CG1 1 
ATOM   1585 C CG2 . VAL   A 1 210 ? -3.447  30.621  0.927   1.00 38.13  ? 207 VAL   A CG2 1 
ATOM   1586 N N   . ILE   A 1 211 ? -7.457  33.085  0.300   1.00 40.91  ? 208 ILE   A N   1 
ATOM   1587 C CA  . ILE   A 1 211 ? -8.306  34.256  0.413   1.00 40.20  ? 208 ILE   A CA  1 
ATOM   1588 C C   . ILE   A 1 211 ? -8.502  34.549  1.880   1.00 44.49  ? 208 ILE   A C   1 
ATOM   1589 O O   . ILE   A 1 211 ? -8.682  33.626  2.680   1.00 44.46  ? 208 ILE   A O   1 
ATOM   1590 C CB  . ILE   A 1 211 ? -9.664  34.024  -0.261  1.00 47.36  ? 208 ILE   A CB  1 
ATOM   1591 C CG1 . ILE   A 1 211 ? -9.482  33.777  -1.754  1.00 41.56  ? 208 ILE   A CG1 1 
ATOM   1592 C CG2 . ILE   A 1 211 ? -10.619 35.183  0.074   1.00 46.11  ? 208 ILE   A CG2 1 
ATOM   1593 C CD1 . ILE   A 1 211 ? -10.698 33.134  -2.392  1.00 47.39  ? 208 ILE   A CD1 1 
ATOM   1594 N N   . ASP   A 1 212 ? -8.482  35.832  2.234   1.00 55.62  ? 209 ASP   A N   1 
ATOM   1595 C CA  . ASP   A 1 212 ? -8.718  36.272  3.605   1.00 51.46  ? 209 ASP   A CA  1 
ATOM   1596 C C   . ASP   A 1 212 ? -10.206 36.534  3.779   1.00 53.78  ? 209 ASP   A C   1 
ATOM   1597 O O   . ASP   A 1 212 ? -10.735 37.500  3.218   1.00 59.96  ? 209 ASP   A O   1 
ATOM   1598 C CB  . ASP   A 1 212 ? -7.908  37.529  3.933   1.00 54.16  ? 209 ASP   A CB  1 
ATOM   1599 C CG  . ASP   A 1 212 ? -7.992  37.905  5.405   1.00 61.11  ? 209 ASP   A CG  1 
ATOM   1600 O OD1 . ASP   A 1 212 ? -9.114  37.952  5.937   1.00 62.31  ? 209 ASP   A OD1 1 
ATOM   1601 O OD2 . ASP   A 1 212 ? -6.937  38.131  6.034   1.00 61.53  ? 209 ASP   A OD2 1 
ATOM   1602 N N   . TYR   A 1 213 ? -10.875 35.674  4.556   1.00 52.83  ? 210 TYR   A N   1 
ATOM   1603 C CA  . TYR   A 1 213 ? -12.318 35.751  4.767   1.00 58.83  ? 210 TYR   A CA  1 
ATOM   1604 C C   . TYR   A 1 213 ? -12.731 36.891  5.692   1.00 62.02  ? 210 TYR   A C   1 
ATOM   1605 O O   . TYR   A 1 213 ? -13.932 37.090  5.909   1.00 61.67  ? 210 TYR   A O   1 
ATOM   1606 C CB  . TYR   A 1 213 ? -12.843 34.425  5.331   1.00 52.63  ? 210 TYR   A CB  1 
ATOM   1607 C CG  . TYR   A 1 213 ? -12.406 34.111  6.752   1.00 61.99  ? 210 TYR   A CG  1 
ATOM   1608 C CD1 . TYR   A 1 213 ? -13.133 34.588  7.853   1.00 64.71  ? 210 TYR   A CD1 1 
ATOM   1609 C CD2 . TYR   A 1 213 ? -11.278 33.329  7.003   1.00 59.47  ? 210 TYR   A CD2 1 
ATOM   1610 C CE1 . TYR   A 1 213 ? -12.737 34.316  9.154   1.00 56.63  ? 210 TYR   A CE1 1 
ATOM   1611 C CE2 . TYR   A 1 213 ? -10.879 33.040  8.311   1.00 58.92  ? 210 TYR   A CE2 1 
ATOM   1612 C CZ  . TYR   A 1 213 ? -11.618 33.535  9.379   1.00 59.40  ? 210 TYR   A CZ  1 
ATOM   1613 O OH  . TYR   A 1 213 ? -11.247 33.231  10.667  1.00 58.32  ? 210 TYR   A OH  1 
ATOM   1614 N N   . LYS   A 1 214 ? -11.776 37.621  6.263   1.00 60.46  ? 211 LYS   A N   1 
ATOM   1615 C CA  . LYS   A 1 214 ? -12.113 38.793  7.063   1.00 65.58  ? 211 LYS   A CA  1 
ATOM   1616 C C   . LYS   A 1 214 ? -12.213 40.059  6.217   1.00 69.87  ? 211 LYS   A C   1 
ATOM   1617 O O   . LYS   A 1 214 ? -13.013 40.947  6.541   1.00 72.97  ? 211 LYS   A O   1 
ATOM   1618 C CB  . LYS   A 1 214 ? -11.093 38.978  8.196   1.00 62.79  ? 211 LYS   A CB  1 
ATOM   1619 C CG  . LYS   A 1 214 ? -11.251 37.957  9.317   1.00 60.44  ? 211 LYS   A CG  1 
ATOM   1620 C CD  . LYS   A 1 214 ? -10.036 37.921  10.228  1.00 66.84  ? 211 LYS   A CD  1 
ATOM   1621 C CE  . LYS   A 1 214 ? -10.224 36.931  11.383  1.00 64.95  ? 211 LYS   A CE  1 
ATOM   1622 N NZ  . LYS   A 1 214 ? -9.034  36.870  12.297  1.00 66.70  ? 211 LYS   A NZ  1 
ATOM   1623 N N   . LEU   A 1 215 ? -11.489 40.121  5.117   1.00 66.33  ? 212 LEU   A N   1 
ATOM   1624 C CA  . LEU   A 1 215 ? -11.668 41.242  4.217   1.00 68.77  ? 212 LEU   A CA  1 
ATOM   1625 C C   . LEU   A 1 215 ? -12.848 40.897  3.311   1.00 73.74  ? 212 LEU   A C   1 
ATOM   1626 O O   . LEU   A 1 215 ? -13.741 41.714  3.112   1.00 72.09  ? 212 LEU   A O   1 
ATOM   1627 C CB  . LEU   A 1 215 ? -10.409 41.514  3.410   1.00 63.64  ? 212 LEU   A CB  1 
ATOM   1628 C CG  . LEU   A 1 215 ? -9.174  41.969  4.181   1.00 66.86  ? 212 LEU   A CG  1 
ATOM   1629 C CD1 . LEU   A 1 215 ? -7.994  42.043  3.230   1.00 64.17  ? 212 LEU   A CD1 1 
ATOM   1630 C CD2 . LEU   A 1 215 ? -9.400  43.312  4.854   1.00 71.32  ? 212 LEU   A CD2 1 
ATOM   1631 N N   . ALA   A 1 216 ? -12.881 39.678  2.788   1.00 70.71  ? 213 ALA   A N   1 
ATOM   1632 C CA  . ALA   A 1 216 ? -13.989 39.254  1.946   1.00 68.18  ? 213 ALA   A CA  1 
ATOM   1633 C C   . ALA   A 1 216 ? -15.202 38.853  2.766   1.00 70.75  ? 213 ALA   A C   1 
ATOM   1634 O O   . ALA   A 1 216 ? -15.543 37.679  2.837   1.00 65.18  ? 213 ALA   A O   1 
ATOM   1635 C CB  . ALA   A 1 216 ? -13.553 38.118  1.067   1.00 57.39  ? 213 ALA   A CB  1 
ATOM   1636 N N   . ASP   A 1 217 ? -15.875 39.831  3.354   1.00 70.85  ? 214 ASP   A N   1 
ATOM   1637 C CA  . ASP   A 1 217 ? -17.017 39.547  4.223   1.00 72.17  ? 214 ASP   A CA  1 
ATOM   1638 C C   . ASP   A 1 217 ? -18.342 39.174  3.555   1.00 70.96  ? 214 ASP   A C   1 
ATOM   1639 O O   . ASP   A 1 217 ? -19.242 38.694  4.225   1.00 73.51  ? 214 ASP   A O   1 
ATOM   1640 C CB  . ASP   A 1 217 ? -17.268 40.762  5.126   1.00 74.48  ? 214 ASP   A CB  1 
ATOM   1641 C CG  . ASP   A 1 217 ? -16.657 42.023  4.590   1.00 74.65  ? 214 ASP   A CG  1 
ATOM   1642 O OD1 . ASP   A 1 217 ? -17.255 42.633  3.686   1.00 74.61  ? 214 ASP   A OD1 1 
ATOM   1643 O OD2 . ASP   A 1 217 ? -15.584 42.413  5.083   1.00 76.55  ? 214 ASP   A OD2 1 
ATOM   1644 N N   . ASP   A 1 218 ? -18.481 39.397  2.258   1.00 72.03  ? 215 ASP   A N   1 
ATOM   1645 C CA  . ASP   A 1 218 ? -19.760 39.152  1.598   1.00 70.08  ? 215 ASP   A CA  1 
ATOM   1646 C C   . ASP   A 1 218 ? -19.578 38.346  0.364   1.00 62.47  ? 215 ASP   A C   1 
ATOM   1647 O O   . ASP   A 1 218 ? -18.533 38.398  -0.248  1.00 63.88  ? 215 ASP   A O   1 
ATOM   1648 C CB  . ASP   A 1 218 ? -20.459 40.472  1.250   1.00 67.97  ? 215 ASP   A CB  1 
ATOM   1649 C CG  . ASP   A 1 218 ? -20.977 41.190  2.458   1.00 72.81  ? 215 ASP   A CG  1 
ATOM   1650 O OD1 . ASP   A 1 218 ? -21.061 40.567  3.529   1.00 75.59  ? 215 ASP   A OD1 1 
ATOM   1651 O OD2 . ASP   A 1 218 ? -21.315 42.377  2.336   1.00 79.22  ? 215 ASP   A OD2 1 
ATOM   1652 N N   . ALA   A 1 219 ? -20.610 37.620  -0.025  1.00 60.45  ? 216 ALA   A N   1 
ATOM   1653 C CA  . ALA   A 1 219 ? -20.507 36.748  -1.168  1.00 57.63  ? 216 ALA   A CA  1 
ATOM   1654 C C   . ALA   A 1 219 ? -20.014 37.545  -2.346  1.00 58.90  ? 216 ALA   A C   1 
ATOM   1655 O O   . ALA   A 1 219 ? -19.361 37.015  -3.216  1.00 56.10  ? 216 ALA   A O   1 
ATOM   1656 C CB  . ALA   A 1 219 ? -21.839 36.110  -1.462  1.00 54.55  ? 216 ALA   A CB  1 
ATOM   1657 N N   . ASP   A 1 220 ? -20.311 38.831  -2.358  1.00 63.00  ? 217 ASP   A N   1 
ATOM   1658 C CA  . ASP   A 1 220 ? -19.845 39.677  -3.427  1.00 64.16  ? 217 ASP   A CA  1 
ATOM   1659 C C   . ASP   A 1 220 ? -18.354 39.870  -3.332  1.00 60.51  ? 217 ASP   A C   1 
ATOM   1660 O O   . ASP   A 1 220 ? -17.635 39.523  -4.251  1.00 55.93  ? 217 ASP   A O   1 
ATOM   1661 C CB  . ASP   A 1 220 ? -20.571 41.010  -3.374  1.00 69.83  ? 217 ASP   A CB  1 
ATOM   1662 C CG  . ASP   A 1 220 ? -21.627 41.137  -4.454  1.00 79.14  ? 217 ASP   A CG  1 
ATOM   1663 O OD1 . ASP   A 1 220 ? -21.766 40.201  -5.269  1.00 75.19  ? 217 ASP   A OD1 1 
ATOM   1664 O OD2 . ASP   A 1 220 ? -22.318 42.175  -4.492  1.00 80.20  ? 217 ASP   A OD2 1 
ATOM   1665 N N   . LYS   A 1 221 ? -17.873 40.441  -2.239  1.00 61.40  ? 218 LYS   A N   1 
ATOM   1666 C CA  . LYS   A 1 221 ? -16.420 40.508  -2.099  1.00 60.61  ? 218 LYS   A CA  1 
ATOM   1667 C C   . LYS   A 1 221 ? -15.808 39.120  -2.232  1.00 56.08  ? 218 LYS   A C   1 
ATOM   1668 O O   . LYS   A 1 221 ? -14.679 38.974  -2.722  1.00 51.93  ? 218 LYS   A O   1 
ATOM   1669 C CB  . LYS   A 1 221 ? -16.035 41.156  -0.759  1.00 64.82  ? 218 LYS   A CB  1 
ATOM   1670 C CG  . LYS   A 1 221 ? -16.396 42.649  -0.619  1.00 72.39  ? 218 LYS   A CG  1 
ATOM   1671 C CD  . LYS   A 1 221 ? -15.981 43.160  0.767   1.00 78.61  ? 218 LYS   A CD  1 
ATOM   1672 C CE  . LYS   A 1 221 ? -16.278 44.640  0.991   1.00 79.19  ? 218 LYS   A CE  1 
ATOM   1673 N NZ  . LYS   A 1 221 ? -15.861 45.042  2.380   1.00 75.97  ? 218 LYS   A NZ  1 
ATOM   1674 N N   . MET   A 1 222 ? -16.557 38.091  -1.826  1.00 53.84  ? 219 MET   A N   1 
ATOM   1675 C CA  . MET   A 1 222 ? -16.076 36.716  -1.887  1.00 50.87  ? 219 MET   A CA  1 
ATOM   1676 C C   . MET   A 1 222 ? -16.058 36.200  -3.322  1.00 50.29  ? 219 MET   A C   1 
ATOM   1677 O O   . MET   A 1 222 ? -15.067 35.598  -3.758  1.00 47.24  ? 219 MET   A O   1 
ATOM   1678 C CB  . MET   A 1 222 ? -16.956 35.832  -0.998  1.00 57.02  ? 219 MET   A CB  1 
ATOM   1679 C CG  . MET   A 1 222 ? -16.338 34.515  -0.525  1.00 55.10  ? 219 MET   A CG  1 
ATOM   1680 S SD  . MET   A 1 222 ? -14.865 34.700  0.482   1.00 62.54  ? 219 MET   A SD  1 
ATOM   1681 C CE  . MET   A 1 222 ? -13.752 33.673  -0.453  1.00 46.08  ? 219 MET   A CE  1 
ATOM   1682 N N   . ARG   A 1 223 ? -17.151 36.421  -4.069  1.00 46.70  ? 220 ARG   A N   1 
ATOM   1683 C CA  . ARG   A 1 223 ? -17.195 36.024  -5.475  1.00 45.39  ? 220 ARG   A CA  1 
ATOM   1684 C C   . ARG   A 1 223 ? -16.022 36.604  -6.244  1.00 48.58  ? 220 ARG   A C   1 
ATOM   1685 O O   . ARG   A 1 223 ? -15.410 35.911  -7.068  1.00 49.87  ? 220 ARG   A O   1 
ATOM   1686 C CB  . ARG   A 1 223 ? -18.517 36.452  -6.124  1.00 46.49  ? 220 ARG   A CB  1 
ATOM   1687 C CG  . ARG   A 1 223 ? -19.552 35.326  -6.240  1.00 50.27  ? 220 ARG   A CG  1 
ATOM   1688 C CD  . ARG   A 1 223 ? -20.894 35.747  -6.859  1.00 50.58  ? 220 ARG   A CD  1 
ATOM   1689 N NE  . ARG   A 1 223 ? -21.638 36.712  -6.054  1.00 55.44  ? 220 ARG   A NE  1 
ATOM   1690 C CZ  . ARG   A 1 223 ? -22.509 36.402  -5.098  1.00 59.69  ? 220 ARG   A CZ  1 
ATOM   1691 N NH1 . ARG   A 1 223 ? -22.742 35.142  -4.749  1.00 58.36  ? 220 ARG   A NH1 1 
ATOM   1692 N NH2 . ARG   A 1 223 ? -23.167 37.380  -4.479  1.00 58.82  ? 220 ARG   A NH2 1 
ATOM   1693 N N   . GLU   A 1 224 ? -15.673 37.866  -5.975  1.00 48.16  ? 221 GLU   A N   1 
ATOM   1694 C CA  . GLU   A 1 224 ? -14.562 38.477  -6.694  1.00 46.96  ? 221 GLU   A CA  1 
ATOM   1695 C C   . GLU   A 1 224 ? -13.234 37.849  -6.302  1.00 43.82  ? 221 GLU   A C   1 
ATOM   1696 O O   . GLU   A 1 224 ? -12.372 37.634  -7.160  1.00 47.80  ? 221 GLU   A O   1 
ATOM   1697 C CB  . GLU   A 1 224 ? -14.539 39.985  -6.463  1.00 50.59  ? 221 GLU   A CB  1 
ATOM   1698 C CG  . GLU   A 1 224 ? -15.511 40.731  -7.370  1.00 59.44  ? 221 GLU   A CG  1 
ATOM   1699 C CD  . GLU   A 1 224 ? -15.324 40.384  -8.856  1.00 71.22  ? 221 GLU   A CD  1 
ATOM   1700 O OE1 . GLU   A 1 224 ? -14.245 40.698  -9.413  1.00 77.98  ? 221 GLU   A OE1 1 
ATOM   1701 O OE2 . GLU   A 1 224 ? -16.245 39.783  -9.466  1.00 67.57  ? 221 GLU   A OE2 1 
ATOM   1702 N N   . ALA   A 1 225 ? -13.055 37.535  -5.017  1.00 45.66  ? 222 ALA   A N   1 
ATOM   1703 C CA  . ALA   A 1 225 ? -11.815 36.904  -4.576  1.00 41.48  ? 222 ALA   A CA  1 
ATOM   1704 C C   . ALA   A 1 225 ? -11.688 35.505  -5.153  1.00 38.60  ? 222 ALA   A C   1 
ATOM   1705 O O   . ALA   A 1 225 ? -10.605 35.097  -5.592  1.00 33.76  ? 222 ALA   A O   1 
ATOM   1706 C CB  . ALA   A 1 225 ? -11.756 36.877  -3.046  1.00 39.25  ? 222 ALA   A CB  1 
ATOM   1707 N N   . LEU   A 1 226 ? -12.795 34.768  -5.198  1.00 40.80  ? 223 LEU   A N   1 
ATOM   1708 C CA  . LEU   A 1 226 ? -12.767 33.443  -5.803  1.00 40.52  ? 223 LEU   A CA  1 
ATOM   1709 C C   . LEU   A 1 226 ? -12.484 33.517  -7.300  1.00 42.86  ? 223 LEU   A C   1 
ATOM   1710 O O   . LEU   A 1 226 ? -11.646 32.769  -7.818  1.00 41.97  ? 223 LEU   A O   1 
ATOM   1711 C CB  . LEU   A 1 226 ? -14.077 32.728  -5.532  1.00 42.87  ? 223 LEU   A CB  1 
ATOM   1712 C CG  . LEU   A 1 226 ? -14.159 32.314  -4.077  1.00 44.00  ? 223 LEU   A CG  1 
ATOM   1713 C CD1 . LEU   A 1 226 ? -15.584 31.967  -3.706  1.00 43.63  ? 223 LEU   A CD1 1 
ATOM   1714 C CD2 . LEU   A 1 226 ? -13.222 31.143  -3.892  1.00 41.09  ? 223 LEU   A CD2 1 
ATOM   1715 N N   . ARG   A 1 227 ? -13.175 34.410  -8.019  1.00 44.58  ? 224 ARG   A N   1 
ATOM   1716 C CA  . ARG   A 1 227 ? -12.942 34.509  -9.456  1.00 41.07  ? 224 ARG   A CA  1 
ATOM   1717 C C   . ARG   A 1 227 ? -11.495 34.863  -9.762  1.00 43.46  ? 224 ARG   A C   1 
ATOM   1718 O O   . ARG   A 1 227 ? -10.953 34.435  -10.791 1.00 45.17  ? 224 ARG   A O   1 
ATOM   1719 C CB  . ARG   A 1 227 ? -13.885 35.529  -10.082 1.00 43.04  ? 224 ARG   A CB  1 
ATOM   1720 C CG  . ARG   A 1 227 ? -15.141 34.916  -10.664 1.00 46.92  ? 224 ARG   A CG  1 
ATOM   1721 C CD  . ARG   A 1 227 ? -15.920 35.940  -11.474 1.00 58.86  ? 224 ARG   A CD  1 
ATOM   1722 N NE  . ARG   A 1 227 ? -16.419 37.012  -10.622 1.00 63.11  ? 224 ARG   A NE  1 
ATOM   1723 C CZ  . ARG   A 1 227 ? -17.561 36.951  -9.948  1.00 65.98  ? 224 ARG   A CZ  1 
ATOM   1724 N NH1 . ARG   A 1 227 ? -18.357 35.892  -10.029 1.00 66.23  ? 224 ARG   A NH1 1 
ATOM   1725 N NH2 . ARG   A 1 227 ? -17.910 37.971  -9.164  1.00 60.71  ? 224 ARG   A NH2 1 
ATOM   1726 N N   . GLU   A 1 228 ? -10.823 35.529  -8.855  1.00 41.52  ? 225 GLU   A N   1 
ATOM   1727 C CA  . GLU   A 1 228 ? -9.427  35.765  -9.103  1.00 39.54  ? 225 GLU   A CA  1 
ATOM   1728 C C   . GLU   A 1 228 ? -8.642  34.510  -8.749  1.00 39.45  ? 225 GLU   A C   1 
ATOM   1729 O O   . GLU   A 1 228 ? -7.847  34.059  -9.543  1.00 39.25  ? 225 GLU   A O   1 
ATOM   1730 C CB  . GLU   A 1 228 ? -8.932  36.984  -8.357  1.00 49.87  ? 225 GLU   A CB  1 
ATOM   1731 C CG  . GLU   A 1 228 ? -7.479  37.328  -8.636  1.00 55.36  ? 225 GLU   A CG  1 
ATOM   1732 C CD  . GLU   A 1 228 ? -7.009  38.583  -7.917  1.00 77.32  ? 225 GLU   A CD  1 
ATOM   1733 O OE1 . GLU   A 1 228 ? -7.796  39.190  -7.156  1.00 73.77  ? 225 GLU   A OE1 1 
ATOM   1734 O OE2 . GLU   A 1 228 ? -5.842  38.975  -8.119  1.00 80.80  ? 225 GLU   A OE2 1 
ATOM   1735 N N   . ALA   A 1 229 ? -8.872  33.937  -7.575  1.00 39.36  ? 226 ALA   A N   1 
ATOM   1736 C CA  . ALA   A 1 229 ? -8.081  32.761  -7.199  1.00 36.82  ? 226 ALA   A CA  1 
ATOM   1737 C C   . ALA   A 1 229 ? -8.415  31.517  -8.017  1.00 37.65  ? 226 ALA   A C   1 
ATOM   1738 O O   . ALA   A 1 229 ? -7.565  30.627  -8.129  1.00 37.69  ? 226 ALA   A O   1 
ATOM   1739 C CB  . ALA   A 1 229 ? -8.260  32.434  -5.718  1.00 33.53  ? 226 ALA   A CB  1 
ATOM   1740 N N   . ALA   A 1 230 ? -9.611  31.436  -8.596  1.00 33.70  ? 227 ALA   A N   1 
ATOM   1741 C CA  . ALA   A 1 230 ? -10.072 30.248  -9.315  1.00 36.73  ? 227 ALA   A CA  1 
ATOM   1742 C C   . ALA   A 1 230 ? -10.708 30.674  -10.635 1.00 37.18  ? 227 ALA   A C   1 
ATOM   1743 O O   . ALA   A 1 230 ? -11.920 30.525  -10.844 1.00 36.02  ? 227 ALA   A O   1 
ATOM   1744 C CB  . ALA   A 1 230 ? -11.051 29.447  -8.450  1.00 32.60  ? 227 ALA   A CB  1 
ATOM   1745 N N   . PRO   A 1 231 ? -9.909  31.201  -11.558 1.00 39.36  ? 228 PRO   A N   1 
ATOM   1746 C CA  . PRO   A 1 231 ? -10.480 31.740  -12.804 1.00 39.89  ? 228 PRO   A CA  1 
ATOM   1747 C C   . PRO   A 1 231 ? -11.130 30.698  -13.697 1.00 39.10  ? 228 PRO   A C   1 
ATOM   1748 O O   . PRO   A 1 231 ? -12.004 31.061  -14.498 1.00 36.32  ? 228 PRO   A O   1 
ATOM   1749 C CB  . PRO   A 1 231 ? -9.273  32.383  -13.492 1.00 36.34  ? 228 PRO   A CB  1 
ATOM   1750 C CG  . PRO   A 1 231 ? -8.101  31.672  -12.911 1.00 38.69  ? 228 PRO   A CG  1 
ATOM   1751 C CD  . PRO   A 1 231 ? -8.452  31.377  -11.498 1.00 38.33  ? 228 PRO   A CD  1 
ATOM   1752 N N   . ASP   A 1 232 ? -10.805 29.437  -13.542 1.00 35.27  ? 229 ASP   A N   1 
ATOM   1753 C CA  . ASP   A 1 232 ? -11.390 28.448  -14.400 1.00 34.53  ? 229 ASP   A CA  1 
ATOM   1754 C C   . ASP   A 1 232 ? -12.555 27.715  -13.754 1.00 33.89  ? 229 ASP   A C   1 
ATOM   1755 O O   . ASP   A 1 232 ? -13.000 26.709  -14.258 1.00 36.31  ? 229 ASP   A O   1 
ATOM   1756 C CB  . ASP   A 1 232 ? -10.312 27.476  -14.846 1.00 42.24  ? 229 ASP   A CB  1 
ATOM   1757 C CG  . ASP   A 1 232 ? -9.339  28.096  -15.825 1.00 48.68  ? 229 ASP   A CG  1 
ATOM   1758 O OD1 . ASP   A 1 232 ? -9.650  29.169  -16.373 1.00 45.84  ? 229 ASP   A OD1 1 
ATOM   1759 O OD2 . ASP   A 1 232 ? -8.262  27.510  -16.049 1.00 44.57  ? 229 ASP   A OD2 1 
ATOM   1760 N N   . GLY   A 1 233 ? -13.051 28.234  -12.651 1.00 31.10  ? 230 GLY   A N   1 
ATOM   1761 C CA  . GLY   A 1 233 ? -14.153 27.605  -11.949 1.00 29.77  ? 230 GLY   A CA  1 
ATOM   1762 C C   . GLY   A 1 233 ? -13.688 26.679  -10.835 1.00 32.73  ? 230 GLY   A C   1 
ATOM   1763 O O   . GLY   A 1 233 ? -12.496 26.459  -10.597 1.00 31.82  ? 230 GLY   A O   1 
ATOM   1764 N N   . VAL   A 1 234 ? -14.669 26.118  -10.133 1.00 31.70  ? 231 VAL   A N   1 
ATOM   1765 C CA  . VAL   A 1 234 ? -14.421 25.238  -9.003  1.00 29.03  ? 231 VAL   A CA  1 
ATOM   1766 C C   . VAL   A 1 234 ? -14.924 23.841  -9.335  1.00 29.22  ? 231 VAL   A C   1 
ATOM   1767 O O   . VAL   A 1 234 ? -16.105 23.667  -9.658  1.00 32.10  ? 231 VAL   A O   1 
ATOM   1768 C CB  . VAL   A 1 234 ? -15.086 25.767  -7.731  1.00 27.19  ? 231 VAL   A CB  1 
ATOM   1769 C CG1 . VAL   A 1 234 ? -14.795 24.825  -6.553  1.00 26.82  ? 231 VAL   A CG1 1 
ATOM   1770 C CG2 . VAL   A 1 234 ? -14.565 27.131  -7.449  1.00 28.80  ? 231 VAL   A CG2 1 
ATOM   1771 N N   . ASP   A 1 235 ? -14.034 22.846  -9.229  1.00 26.67  ? 232 ASP   A N   1 
ATOM   1772 C CA  . ASP   A 1 235 ? -14.405 21.450  -9.432  1.00 28.79  ? 232 ASP   A CA  1 
ATOM   1773 C C   . ASP   A 1 235 ? -14.697 20.719  -8.134  1.00 28.49  ? 232 ASP   A C   1 
ATOM   1774 O O   . ASP   A 1 235 ? -15.590 19.875  -8.108  1.00 29.93  ? 232 ASP   A O   1 
ATOM   1775 C CB  . ASP   A 1 235 ? -13.314 20.690  -10.190 1.00 26.38  ? 232 ASP   A CB  1 
ATOM   1776 C CG  . ASP   A 1 235 ? -12.779 21.469  -11.368 1.00 31.37  ? 232 ASP   A CG  1 
ATOM   1777 O OD1 . ASP   A 1 235 ? -13.493 21.589  -12.392 1.00 31.13  ? 232 ASP   A OD1 1 
ATOM   1778 O OD2 . ASP   A 1 235 ? -11.649 21.991  -11.257 1.00 30.32  ? 232 ASP   A OD2 1 
ATOM   1779 N N   . LYS   A 1 236 ? -13.952 20.979  -7.062  1.00 28.90  ? 233 LYS   A N   1 
ATOM   1780 C CA  . LYS   A 1 236 ? -14.275 20.390  -5.771  1.00 28.23  ? 233 LYS   A CA  1 
ATOM   1781 C C   . LYS   A 1 236 ? -14.272 21.485  -4.727  1.00 29.08  ? 233 LYS   A C   1 
ATOM   1782 O O   . LYS   A 1 236 ? -13.499 22.441  -4.815  1.00 30.91  ? 233 LYS   A O   1 
ATOM   1783 C CB  . LYS   A 1 236 ? -13.300 19.281  -5.302  1.00 26.07  ? 233 LYS   A CB  1 
ATOM   1784 C CG  . LYS   A 1 236 ? -12.662 18.472  -6.380  1.00 31.49  ? 233 LYS   A CG  1 
ATOM   1785 C CD  . LYS   A 1 236 ? -13.590 17.480  -7.027  1.00 34.51  ? 233 LYS   A CD  1 
ATOM   1786 C CE  . LYS   A 1 236 ? -12.918 16.993  -8.298  1.00 34.64  ? 233 LYS   A CE  1 
ATOM   1787 N NZ  . LYS   A 1 236 ? -13.531 15.803  -8.905  1.00 33.02  ? 233 LYS   A NZ  1 
ATOM   1788 N N   . TYR   A 1 237 ? -15.131 21.306  -3.727  1.00 25.55  ? 234 TYR   A N   1 
ATOM   1789 C CA  . TYR   A 1 237 ? -15.241 22.204  -2.589  1.00 27.05  ? 234 TYR   A CA  1 
ATOM   1790 C C   . TYR   A 1 237 ? -15.316 21.372  -1.309  1.00 30.01  ? 234 TYR   A C   1 
ATOM   1791 O O   . TYR   A 1 237 ? -16.238 20.564  -1.147  1.00 23.97  ? 234 TYR   A O   1 
ATOM   1792 C CB  . TYR   A 1 237 ? -16.489 23.075  -2.724  1.00 27.79  ? 234 TYR   A CB  1 
ATOM   1793 C CG  . TYR   A 1 237 ? -16.681 24.088  -1.615  1.00 28.69  ? 234 TYR   A CG  1 
ATOM   1794 C CD1 . TYR   A 1 237 ? -15.585 24.663  -0.970  1.00 26.68  ? 234 TYR   A CD1 1 
ATOM   1795 C CD2 . TYR   A 1 237 ? -17.958 24.477  -1.220  1.00 25.11  ? 234 TYR   A CD2 1 
ATOM   1796 C CE1 . TYR   A 1 237 ? -15.761 25.598  0.037   1.00 29.40  ? 234 TYR   A CE1 1 
ATOM   1797 C CE2 . TYR   A 1 237 ? -18.141 25.422  -0.225  1.00 28.42  ? 234 TYR   A CE2 1 
ATOM   1798 C CZ  . TYR   A 1 237 ? -17.036 25.976  0.403   1.00 28.10  ? 234 TYR   A CZ  1 
ATOM   1799 O OH  . TYR   A 1 237 ? -17.197 26.911  1.389   1.00 26.87  ? 234 TYR   A OH  1 
ATOM   1800 N N   . PHE   A 1 238 ? -14.344 21.551  -0.403  1.00 27.60  ? 235 PHE   A N   1 
ATOM   1801 C CA  . PHE   A 1 238 ? -14.420 20.984  0.939   1.00 29.72  ? 235 PHE   A CA  1 
ATOM   1802 C C   . PHE   A 1 238 ? -14.823 22.133  1.861   1.00 30.64  ? 235 PHE   A C   1 
ATOM   1803 O O   . PHE   A 1 238 ? -14.086 23.119  1.998   1.00 25.90  ? 235 PHE   A O   1 
ATOM   1804 C CB  . PHE   A 1 238 ? -13.103 20.330  1.364   1.00 26.69  ? 235 PHE   A CB  1 
ATOM   1805 C CG  . PHE   A 1 238 ? -13.220 19.484  2.609   1.00 27.32  ? 235 PHE   A CG  1 
ATOM   1806 C CD1 . PHE   A 1 238 ? -13.125 20.059  3.884   1.00 30.15  ? 235 PHE   A CD1 1 
ATOM   1807 C CD2 . PHE   A 1 238 ? -13.427 18.112  2.516   1.00 28.73  ? 235 PHE   A CD2 1 
ATOM   1808 C CE1 . PHE   A 1 238 ? -13.230 19.271  5.036   1.00 26.22  ? 235 PHE   A CE1 1 
ATOM   1809 C CE2 . PHE   A 1 238 ? -13.544 17.320  3.664   1.00 27.60  ? 235 PHE   A CE2 1 
ATOM   1810 C CZ  . PHE   A 1 238 ? -13.445 17.904  4.924   1.00 25.36  ? 235 PHE   A CZ  1 
ATOM   1811 N N   . ASP   A 1 239 ? -16.009 22.022  2.452   1.00 26.27  ? 236 ASP   A N   1 
ATOM   1812 C CA  . ASP   A 1 239 ? -16.670 23.140  3.115   1.00 33.10  ? 236 ASP   A CA  1 
ATOM   1813 C C   . ASP   A 1 239 ? -16.752 22.895  4.617   1.00 33.76  ? 236 ASP   A C   1 
ATOM   1814 O O   . ASP   A 1 239 ? -17.428 21.961  5.054   1.00 34.11  ? 236 ASP   A O   1 
ATOM   1815 C CB  . ASP   A 1 239 ? -18.073 23.339  2.538   1.00 32.37  ? 236 ASP   A CB  1 
ATOM   1816 C CG  . ASP   A 1 239 ? -18.758 24.600  3.066   1.00 37.27  ? 236 ASP   A CG  1 
ATOM   1817 O OD1 . ASP   A 1 239 ? -18.071 25.469  3.672   1.00 36.20  ? 236 ASP   A OD1 1 
ATOM   1818 O OD2 . ASP   A 1 239 ? -19.990 24.729  2.862   1.00 36.72  ? 236 ASP   A OD2 1 
ATOM   1819 N N   . SER   A 1 240 ? -16.090 23.737  5.408   1.00 32.82  ? 237 SER   A N   1 
ATOM   1820 C CA  . SER   A 1 240 ? -16.284 23.710  6.857   1.00 39.61  ? 237 SER   A CA  1 
ATOM   1821 C C   . SER   A 1 240 ? -16.978 24.956  7.387   1.00 38.96  ? 237 SER   A C   1 
ATOM   1822 O O   . SER   A 1 240 ? -17.189 25.061  8.603   1.00 39.68  ? 237 SER   A O   1 
ATOM   1823 C CB  . SER   A 1 240 ? -14.946 23.527  7.586   1.00 35.76  ? 237 SER   A CB  1 
ATOM   1824 O OG  . SER   A 1 240 ? -14.514 22.185  7.482   1.00 40.99  ? 237 SER   A OG  1 
ATOM   1825 N N   . ILE   A 1 241 ? -17.359 25.888  6.510   1.00 37.64  ? 238 ILE   A N   1 
ATOM   1826 C CA  . ILE   A 1 241 ? -17.764 27.232  6.901   1.00 38.51  ? 238 ILE   A CA  1 
ATOM   1827 C C   . ILE   A 1 241 ? -19.225 27.508  6.564   1.00 37.68  ? 238 ILE   A C   1 
ATOM   1828 O O   . ILE   A 1 241 ? -19.972 28.016  7.397   1.00 38.31  ? 238 ILE   A O   1 
ATOM   1829 C CB  . ILE   A 1 241 ? -16.848 28.293  6.268   1.00 38.64  ? 238 ILE   A CB  1 
ATOM   1830 C CG1 . ILE   A 1 241 ? -15.420 28.059  6.752   1.00 45.52  ? 238 ILE   A CG1 1 
ATOM   1831 C CG2 . ILE   A 1 241 ? -17.325 29.676  6.621   1.00 37.70  ? 238 ILE   A CG2 1 
ATOM   1832 C CD1 . ILE   A 1 241 ? -15.303 27.950  8.277   1.00 43.63  ? 238 ILE   A CD1 1 
ATOM   1833 N N   . GLY   A 1 242 ? -19.645 27.202  5.336   1.00 36.69  ? 239 GLY   A N   1 
ATOM   1834 C CA  . GLY   A 1 242 ? -20.992 27.594  4.955   1.00 35.73  ? 239 GLY   A CA  1 
ATOM   1835 C C   . GLY   A 1 242 ? -21.116 29.110  4.853   1.00 38.30  ? 239 GLY   A C   1 
ATOM   1836 O O   . GLY   A 1 242 ? -20.128 29.833  4.665   1.00 37.96  ? 239 GLY   A O   1 
ATOM   1837 N N   . GLY   A 1 243 ? -22.349 29.601  4.992   1.00 40.39  ? 240 GLY   A N   1 
ATOM   1838 C CA  . GLY   A 1 243 ? -22.566 31.034  4.893   1.00 38.90  ? 240 GLY   A CA  1 
ATOM   1839 C C   . GLY   A 1 243 ? -22.179 31.581  3.528   1.00 45.30  ? 240 GLY   A C   1 
ATOM   1840 O O   . GLY   A 1 243 ? -22.391 30.945  2.481   1.00 43.00  ? 240 GLY   A O   1 
ATOM   1841 N N   . SER   A 1 244 ? -21.559 32.768  3.544   1.00 45.21  ? 241 SER   A N   1 
ATOM   1842 C CA  . SER   A 1 244 ? -21.393 33.552  2.324   1.00 43.83  ? 241 SER   A CA  1 
ATOM   1843 C C   . SER   A 1 244 ? -20.293 32.996  1.424   1.00 40.93  ? 241 SER   A C   1 
ATOM   1844 O O   . SER   A 1 244 ? -20.399 33.087  0.191   1.00 42.47  ? 241 SER   A O   1 
ATOM   1845 C CB  . SER   A 1 244 ? -21.105 35.017  2.674   1.00 45.93  ? 241 SER   A CB  1 
ATOM   1846 O OG  . SER   A 1 244 ? -19.706 35.242  2.720   1.00 52.97  ? 241 SER   A OG  1 
ATOM   1847 N N   . VAL   A 1 245 ? -19.232 32.431  2.006   1.00 32.80  ? 242 VAL   A N   1 
ATOM   1848 C CA  . VAL   A 1 245 ? -18.193 31.829  1.176   1.00 35.47  ? 242 VAL   A CA  1 
ATOM   1849 C C   . VAL   A 1 245 ? -18.759 30.649  0.392   1.00 34.62  ? 242 VAL   A C   1 
ATOM   1850 O O   . VAL   A 1 245 ? -18.472 30.484  -0.796  1.00 34.86  ? 242 VAL   A O   1 
ATOM   1851 C CB  . VAL   A 1 245 ? -16.971 31.427  2.026   1.00 36.72  ? 242 VAL   A CB  1 
ATOM   1852 C CG1 . VAL   A 1 245 ? -17.347 30.431  3.091   1.00 35.93  ? 242 VAL   A CG1 1 
ATOM   1853 C CG2 . VAL   A 1 245 ? -15.860 30.861  1.139   1.00 33.57  ? 242 VAL   A CG2 1 
ATOM   1854 N N   . THR   A 1 246 ? -19.588 29.827  1.030   1.00 33.13  ? 243 THR   A N   1 
ATOM   1855 C CA  . THR   A 1 246 ? -20.221 28.727  0.317   1.00 35.74  ? 243 THR   A CA  1 
ATOM   1856 C C   . THR   A 1 246 ? -21.216 29.240  -0.716  1.00 37.45  ? 243 THR   A C   1 
ATOM   1857 O O   . THR   A 1 246 ? -21.333 28.667  -1.808  1.00 34.72  ? 243 THR   A O   1 
ATOM   1858 C CB  . THR   A 1 246 ? -20.910 27.788  1.307   1.00 34.70  ? 243 THR   A CB  1 
ATOM   1859 O OG1 . THR   A 1 246 ? -19.914 27.027  2.006   1.00 34.07  ? 243 THR   A OG1 1 
ATOM   1860 C CG2 . THR   A 1 246 ? -21.875 26.852  0.600   1.00 27.27  ? 243 THR   A CG2 1 
ATOM   1861 N N   . ASP   A 1 247 ? -21.943 30.318  -0.398  1.00 39.25  ? 244 ASP   A N   1 
ATOM   1862 C CA  . ASP   A 1 247 ? -22.828 30.898  -1.407  1.00 40.56  ? 244 ASP   A CA  1 
ATOM   1863 C C   . ASP   A 1 247 ? -22.031 31.310  -2.639  1.00 35.99  ? 244 ASP   A C   1 
ATOM   1864 O O   . ASP   A 1 247 ? -22.481 31.116  -3.770  1.00 34.88  ? 244 ASP   A O   1 
ATOM   1865 C CB  . ASP   A 1 247 ? -23.587 32.114  -0.854  1.00 42.79  ? 244 ASP   A CB  1 
ATOM   1866 C CG  . ASP   A 1 247 ? -24.628 31.762  0.236   1.00 48.35  ? 244 ASP   A CG  1 
ATOM   1867 O OD1 . ASP   A 1 247 ? -25.211 30.643  0.253   1.00 47.75  ? 244 ASP   A OD1 1 
ATOM   1868 O OD2 . ASP   A 1 247 ? -24.878 32.656  1.078   1.00 46.49  ? 244 ASP   A OD2 1 
ATOM   1869 N N   . ALA   A 1 248 ? -20.831 31.861  -2.436  1.00 34.10  ? 245 ALA   A N   1 
ATOM   1870 C CA  . ALA   A 1 248 ? -20.044 32.317  -3.572  1.00 35.80  ? 245 ALA   A CA  1 
ATOM   1871 C C   . ALA   A 1 248 ? -19.523 31.141  -4.386  1.00 33.36  ? 245 ALA   A C   1 
ATOM   1872 O O   . ALA   A 1 248 ? -19.480 31.204  -5.621  1.00 36.34  ? 245 ALA   A O   1 
ATOM   1873 C CB  . ALA   A 1 248 ? -18.896 33.204  -3.092  1.00 38.27  ? 245 ALA   A CB  1 
ATOM   1874 N N   . VAL   A 1 249 ? -19.127 30.057  -3.721  1.00 29.78  ? 246 VAL   A N   1 
ATOM   1875 C CA  . VAL   A 1 249 ? -18.574 28.922  -4.445  1.00 31.04  ? 246 VAL   A CA  1 
ATOM   1876 C C   . VAL   A 1 249 ? -19.640 28.299  -5.326  1.00 31.22  ? 246 VAL   A C   1 
ATOM   1877 O O   . VAL   A 1 249 ? -19.371 27.888  -6.459  1.00 29.26  ? 246 VAL   A O   1 
ATOM   1878 C CB  . VAL   A 1 249 ? -17.974 27.894  -3.468  1.00 32.42  ? 246 VAL   A CB  1 
ATOM   1879 C CG1 . VAL   A 1 249 ? -17.600 26.643  -4.203  1.00 27.79  ? 246 VAL   A CG1 1 
ATOM   1880 C CG2 . VAL   A 1 249 ? -16.758 28.457  -2.754  1.00 29.59  ? 246 VAL   A CG2 1 
ATOM   1881 N N   . PHE   A 1 250 ? -20.876 28.249  -4.838  1.00 33.64  ? 247 PHE   A N   1 
ATOM   1882 C CA  . PHE   A 1 250 ? -21.922 27.605  -5.618  1.00 33.32  ? 247 PHE   A CA  1 
ATOM   1883 C C   . PHE   A 1 250 ? -22.285 28.375  -6.878  1.00 33.63  ? 247 PHE   A C   1 
ATOM   1884 O O   . PHE   A 1 250 ? -22.938 27.801  -7.758  1.00 39.00  ? 247 PHE   A O   1 
ATOM   1885 C CB  . PHE   A 1 250 ? -23.158 27.392  -4.764  1.00 28.96  ? 247 PHE   A CB  1 
ATOM   1886 C CG  . PHE   A 1 250 ? -23.156 26.098  -4.043  1.00 30.23  ? 247 PHE   A CG  1 
ATOM   1887 C CD1 . PHE   A 1 250 ? -22.159 25.808  -3.126  1.00 27.89  ? 247 PHE   A CD1 1 
ATOM   1888 C CD2 . PHE   A 1 250 ? -24.156 25.162  -4.277  1.00 33.97  ? 247 PHE   A CD2 1 
ATOM   1889 C CE1 . PHE   A 1 250 ? -22.160 24.617  -2.455  1.00 31.00  ? 247 PHE   A CE1 1 
ATOM   1890 C CE2 . PHE   A 1 250 ? -24.169 23.952  -3.611  1.00 30.08  ? 247 PHE   A CE2 1 
ATOM   1891 C CZ  . PHE   A 1 250 ? -23.172 23.674  -2.699  1.00 31.46  ? 247 PHE   A CZ  1 
ATOM   1892 N N   . SER   A 1 251 ? -21.871 29.636  -7.001  1.00 30.61  ? 248 SER   A N   1 
ATOM   1893 C CA  . SER   A 1 251 ? -22.102 30.360  -8.245  1.00 37.41  ? 248 SER   A CA  1 
ATOM   1894 C C   . SER   A 1 251 ? -21.099 30.015  -9.345  1.00 34.62  ? 248 SER   A C   1 
ATOM   1895 O O   . SER   A 1 251 ? -21.344 30.360  -10.499 1.00 33.72  ? 248 SER   A O   1 
ATOM   1896 C CB  . SER   A 1 251 ? -22.064 31.865  -8.004  1.00 31.15  ? 248 SER   A CB  1 
ATOM   1897 O OG  . SER   A 1 251 ? -20.752 32.269  -7.706  1.00 38.90  ? 248 SER   A OG  1 
ATOM   1898 N N   . MET   A 1 252 ? -19.997 29.339  -9.032  1.00 32.10  ? 249 MET   A N   1 
ATOM   1899 C CA  . MET   A 1 252 ? -18.952 29.064  -10.009 1.00 28.67  ? 249 MET   A CA  1 
ATOM   1900 C C   . MET   A 1 252 ? -18.616 27.581  -10.047 1.00 25.96  ? 249 MET   A C   1 
ATOM   1901 O O   . MET   A 1 252 ? -17.468 27.190  -10.255 1.00 29.53  ? 249 MET   A O   1 
ATOM   1902 C CB  . MET   A 1 252 ? -17.712 29.896  -9.711  1.00 24.56  ? 249 MET   A CB  1 
ATOM   1903 C CG  . MET   A 1 252 ? -17.222 29.734  -8.272  1.00 33.84  ? 249 MET   A CG  1 
ATOM   1904 S SD  . MET   A 1 252 ? -16.066 31.050  -7.794  1.00 44.98  ? 249 MET   A SD  1 
ATOM   1905 C CE  . MET   A 1 252 ? -17.042 32.467  -8.225  1.00 38.29  ? 249 MET   A CE  1 
ATOM   1906 N N   . LEU   A 1 253 ? -19.612 26.730  -9.861  1.00 25.75  ? 250 LEU   A N   1 
ATOM   1907 C CA  . LEU   A 1 253 ? -19.396 25.289  -9.889  1.00 28.82  ? 250 LEU   A CA  1 
ATOM   1908 C C   . LEU   A 1 253 ? -19.285 24.785  -11.322 1.00 32.82  ? 250 LEU   A C   1 
ATOM   1909 O O   . LEU   A 1 253 ? -20.178 25.022  -12.144 1.00 32.57  ? 250 LEU   A O   1 
ATOM   1910 C CB  . LEU   A 1 253 ? -20.535 24.569  -9.173  1.00 26.82  ? 250 LEU   A CB  1 
ATOM   1911 C CG  . LEU   A 1 253 ? -20.553 24.681  -7.643  1.00 32.67  ? 250 LEU   A CG  1 
ATOM   1912 C CD1 . LEU   A 1 253 ? -21.890 24.200  -7.147  1.00 30.22  ? 250 LEU   A CD1 1 
ATOM   1913 C CD2 . LEU   A 1 253 ? -19.419 23.875  -6.988  1.00 22.63  ? 250 LEU   A CD2 1 
ATOM   1914 N N   . ASN   A 1 254 ? -18.193 24.077  -11.613 1.00 29.38  ? 251 ASN   A N   1 
ATOM   1915 C CA  . ASN   A 1 254 ? -17.976 23.454  -12.914 1.00 28.76  ? 251 ASN   A CA  1 
ATOM   1916 C C   . ASN   A 1 254 ? -18.808 22.180  -13.048 1.00 30.51  ? 251 ASN   A C   1 
ATOM   1917 O O   . ASN   A 1 254 ? -19.492 21.738  -12.117 1.00 30.30  ? 251 ASN   A O   1 
ATOM   1918 C CB  . ASN   A 1 254 ? -16.497 23.119  -13.126 1.00 31.77  ? 251 ASN   A CB  1 
ATOM   1919 C CG  . ASN   A 1 254 ? -15.627 24.351  -13.282 1.00 28.98  ? 251 ASN   A CG  1 
ATOM   1920 O OD1 . ASN   A 1 254 ? -16.104 25.394  -13.676 1.00 33.60  ? 251 ASN   A OD1 1 
ATOM   1921 N ND2 . ASN   A 1 254 ? -14.342 24.223  -12.990 1.00 27.63  ? 251 ASN   A ND2 1 
ATOM   1922 N N   . VAL   A 1 255 ? -18.725 21.572  -14.227 1.00 30.88  ? 252 VAL   A N   1 
ATOM   1923 C CA  . VAL   A 1 255 ? -19.556 20.424  -14.563 1.00 28.60  ? 252 VAL   A CA  1 
ATOM   1924 C C   . VAL   A 1 255 ? -18.969 19.168  -13.927 1.00 29.47  ? 252 VAL   A C   1 
ATOM   1925 O O   . VAL   A 1 255 ? -17.759 18.928  -13.989 1.00 29.23  ? 252 VAL   A O   1 
ATOM   1926 C CB  . VAL   A 1 255 ? -19.692 20.300  -16.090 1.00 26.82  ? 252 VAL   A CB  1 
ATOM   1927 C CG1 . VAL   A 1 255 ? -20.153 18.892  -16.516 1.00 21.00  ? 252 VAL   A CG1 1 
ATOM   1928 C CG2 . VAL   A 1 255 ? -20.653 21.345  -16.584 1.00 21.73  ? 252 VAL   A CG2 1 
ATOM   1929 N N   . GLY   A 1 256 ? -19.826 18.364  -13.306 1.00 29.35  ? 253 GLY   A N   1 
ATOM   1930 C CA  . GLY   A 1 256 ? -19.328 17.225  -12.566 1.00 29.24  ? 253 GLY   A CA  1 
ATOM   1931 C C   . GLY   A 1 256 ? -18.597 17.592  -11.292 1.00 30.17  ? 253 GLY   A C   1 
ATOM   1932 O O   . GLY   A 1 256 ? -17.765 16.824  -10.825 1.00 27.11  ? 253 GLY   A O   1 
ATOM   1933 N N   . SER   A 1 257 ? -18.874 18.756  -10.714 1.00 30.18  ? 254 SER   A N   1 
ATOM   1934 C CA  . SER   A 1 257 ? -18.195 19.124  -9.482  1.00 32.13  ? 254 SER   A CA  1 
ATOM   1935 C C   . SER   A 1 257 ? -18.689 18.270  -8.302  1.00 31.37  ? 254 SER   A C   1 
ATOM   1936 O O   . SER   A 1 257 ? -19.708 17.566  -8.386  1.00 30.24  ? 254 SER   A O   1 
ATOM   1937 C CB  . SER   A 1 257 ? -18.395 20.612  -9.212  1.00 29.63  ? 254 SER   A CB  1 
ATOM   1938 O OG  . SER   A 1 257 ? -19.746 20.979  -9.449  1.00 32.66  ? 254 SER   A OG  1 
ATOM   1939 N N   . GLN   A 1 258 ? -17.926 18.307  -7.204  1.00 24.49  ? 255 GLN   A N   1 
ATOM   1940 C CA  . GLN   A 1 258 ? -18.299 17.630  -5.960  1.00 28.02  ? 255 GLN   A CA  1 
ATOM   1941 C C   . GLN   A 1 258 ? -18.056 18.543  -4.771  1.00 26.99  ? 255 GLN   A C   1 
ATOM   1942 O O   . GLN   A 1 258 ? -16.969 19.126  -4.644  1.00 28.97  ? 255 GLN   A O   1 
ATOM   1943 C CB  . GLN   A 1 258 ? -17.514 16.337  -5.721  1.00 29.27  ? 255 GLN   A CB  1 
ATOM   1944 C CG  . GLN   A 1 258 ? -17.574 15.292  -6.812  1.00 27.83  ? 255 GLN   A CG  1 
ATOM   1945 C CD  . GLN   A 1 258 ? -16.586 14.169  -6.543  1.00 31.15  ? 255 GLN   A CD  1 
ATOM   1946 O OE1 . GLN   A 1 258 ? -15.374 14.358  -6.659  1.00 33.32  ? 255 GLN   A OE1 1 
ATOM   1947 N NE2 . GLN   A 1 258 ? -17.095 13.005  -6.156  1.00 30.79  ? 255 GLN   A NE2 1 
ATOM   1948 N N   . VAL   A 1 259 ? -19.044 18.616  -3.876  1.00 23.81  ? 256 VAL   A N   1 
ATOM   1949 C CA  . VAL   A 1 259 ? -18.970 19.393  -2.646  1.00 25.48  ? 256 VAL   A CA  1 
ATOM   1950 C C   . VAL   A 1 259 ? -19.085 18.446  -1.445  1.00 29.94  ? 256 VAL   A C   1 
ATOM   1951 O O   . VAL   A 1 259 ? -20.044 17.668  -1.342  1.00 27.22  ? 256 VAL   A O   1 
ATOM   1952 C CB  . VAL   A 1 259 ? -20.070 20.467  -2.612  1.00 28.34  ? 256 VAL   A CB  1 
ATOM   1953 C CG1 . VAL   A 1 259 ? -20.019 21.248  -1.311  1.00 24.51  ? 256 VAL   A CG1 1 
ATOM   1954 C CG2 . VAL   A 1 259 ? -19.936 21.408  -3.825  1.00 27.63  ? 256 VAL   A CG2 1 
ATOM   1955 N N   . ALA   A 1 260 ? -18.107 18.503  -0.540  1.00 25.10  ? 257 ALA   A N   1 
ATOM   1956 C CA  . ALA   A 1 260 ? -18.175 17.766  0.720   1.00 25.19  ? 257 ALA   A CA  1 
ATOM   1957 C C   . ALA   A 1 260 ? -18.483 18.746  1.850   1.00 26.10  ? 257 ALA   A C   1 
ATOM   1958 O O   . ALA   A 1 260 ? -17.723 19.690  2.085   1.00 24.90  ? 257 ALA   A O   1 
ATOM   1959 C CB  . ALA   A 1 260 ? -16.878 17.000  0.985   1.00 18.58  ? 257 ALA   A CB  1 
ATOM   1960 N N   . VAL   A 1 261 ? -19.594 18.528  2.542   1.00 27.78  ? 258 VAL   A N   1 
ATOM   1961 C CA  . VAL   A 1 261 ? -20.013 19.394  3.638   1.00 32.47  ? 258 VAL   A CA  1 
ATOM   1962 C C   . VAL   A 1 261 ? -19.586 18.739  4.942   1.00 31.32  ? 258 VAL   A C   1 
ATOM   1963 O O   . VAL   A 1 261 ? -20.148 17.724  5.360   1.00 29.73  ? 258 VAL   A O   1 
ATOM   1964 C CB  . VAL   A 1 261 ? -21.521 19.662  3.611   1.00 33.35  ? 258 VAL   A CB  1 
ATOM   1965 C CG1 . VAL   A 1 261 ? -21.882 20.633  4.710   1.00 28.97  ? 258 VAL   A CG1 1 
ATOM   1966 C CG2 . VAL   A 1 261 ? -21.902 20.222  2.253   1.00 31.23  ? 258 VAL   A CG2 1 
ATOM   1967 N N   . CYS   A 1 262 ? -18.584 19.335  5.576   1.00 33.38  ? 259 CYS   A N   1 
ATOM   1968 C CA  . CYS   A 1 262 ? -17.976 18.841  6.800   1.00 37.13  ? 259 CYS   A CA  1 
ATOM   1969 C C   . CYS   A 1 262 ? -18.443 19.611  8.029   1.00 37.00  ? 259 CYS   A C   1 
ATOM   1970 O O   . CYS   A 1 262 ? -18.614 19.021  9.098   1.00 41.43  ? 259 CYS   A O   1 
ATOM   1971 C CB  . CYS   A 1 262 ? -16.446 18.899  6.652   1.00 36.65  ? 259 CYS   A CB  1 
ATOM   1972 S SG  . CYS   A 1 262 ? -15.447 18.495  8.095   1.00 45.39  ? 259 CYS   A SG  1 
ATOM   1973 N N   . TRP   A 1 263 ? -18.681 20.911  7.903   1.00 38.25  ? 260 TRP   A N   1 
ATOM   1974 C CA  . TRP   A 1 263 ? -19.213 21.707  9.005   1.00 39.73  ? 260 TRP   A CA  1 
ATOM   1975 C C   . TRP   A 1 263 ? -19.797 22.983  8.415   1.00 40.23  ? 260 TRP   A C   1 
ATOM   1976 O O   . TRP   A 1 263 ? -19.531 23.336  7.261   1.00 38.71  ? 260 TRP   A O   1 
ATOM   1977 C CB  . TRP   A 1 263 ? -18.135 22.018  10.070  1.00 40.70  ? 260 TRP   A CB  1 
ATOM   1978 C CG  . TRP   A 1 263 ? -18.675 21.999  11.509  1.00 46.15  ? 260 TRP   A CG  1 
ATOM   1979 C CD1 . TRP   A 1 263 ? -19.431 21.007  12.089  1.00 41.70  ? 260 TRP   A CD1 1 
ATOM   1980 C CD2 . TRP   A 1 263 ? -18.510 23.009  12.522  1.00 41.22  ? 260 TRP   A CD2 1 
ATOM   1981 N NE1 . TRP   A 1 263 ? -19.749 21.345  13.377  1.00 39.25  ? 260 TRP   A NE1 1 
ATOM   1982 C CE2 . TRP   A 1 263 ? -19.195 22.562  13.675  1.00 39.90  ? 260 TRP   A CE2 1 
ATOM   1983 C CE3 . TRP   A 1 263 ? -17.861 24.245  12.565  1.00 41.67  ? 260 TRP   A CE3 1 
ATOM   1984 C CZ2 . TRP   A 1 263 ? -19.242 23.304  14.860  1.00 38.05  ? 260 TRP   A CZ2 1 
ATOM   1985 C CZ3 . TRP   A 1 263 ? -17.915 24.992  13.762  1.00 42.48  ? 260 TRP   A CZ3 1 
ATOM   1986 C CH2 . TRP   A 1 263 ? -18.598 24.513  14.882  1.00 36.46  ? 260 TRP   A CH2 1 
ATOM   1987 N N   . GLN   A 1 264 ? -20.611 23.669  9.217   1.00 39.04  ? 261 GLN   A N   1 
ATOM   1988 C CA  . GLN   A 1 264 ? -21.213 24.942  8.824   1.00 33.42  ? 261 GLN   A CA  1 
ATOM   1989 C C   . GLN   A 1 264 ? -21.020 25.960  9.944   1.00 39.86  ? 261 GLN   A C   1 
ATOM   1990 O O   . GLN   A 1 264 ? -21.975 26.456  10.541  1.00 42.42  ? 261 GLN   A O   1 
ATOM   1991 C CB  . GLN   A 1 264 ? -22.689 24.780  8.492   1.00 31.75  ? 261 GLN   A CB  1 
ATOM   1992 C CG  . GLN   A 1 264 ? -22.985 23.893  7.296   1.00 38.11  ? 261 GLN   A CG  1 
ATOM   1993 C CD  . GLN   A 1 264 ? -22.617 24.545  5.966   1.00 40.62  ? 261 GLN   A CD  1 
ATOM   1994 O OE1 . GLN   A 1 264 ? -23.471 25.112  5.281   1.00 50.80  ? 261 GLN   A OE1 1 
ATOM   1995 N NE2 . GLN   A 1 264 ? -21.348 24.457  5.591   1.00 37.14  ? 261 GLN   A NE2 1 
ATOM   1996 N N   . TRP   A 1 265 ? -19.755 26.255  10.242  1.00 36.60  ? 262 TRP   A N   1 
ATOM   1997 C CA  . TRP   A 1 265 ? -19.375 27.247  11.239  1.00 39.95  ? 262 TRP   A CA  1 
ATOM   1998 C C   . TRP   A 1 265 ? -20.248 28.496  11.207  1.00 45.25  ? 262 TRP   A C   1 
ATOM   1999 O O   . TRP   A 1 265 ? -20.675 28.999  12.254  1.00 46.93  ? 262 TRP   A O   1 
ATOM   2000 C CB  . TRP   A 1 265 ? -17.923 27.639  11.011  1.00 39.52  ? 262 TRP   A CB  1 
ATOM   2001 C CG  . TRP   A 1 265 ? -17.366 28.625  11.968  1.00 47.63  ? 262 TRP   A CG  1 
ATOM   2002 C CD1 . TRP   A 1 265 ? -17.791 29.910  12.195  1.00 47.06  ? 262 TRP   A CD1 1 
ATOM   2003 C CD2 . TRP   A 1 265 ? -16.227 28.427  12.806  1.00 48.93  ? 262 TRP   A CD2 1 
ATOM   2004 N NE1 . TRP   A 1 265 ? -16.993 30.509  13.140  1.00 47.06  ? 262 TRP   A NE1 1 
ATOM   2005 C CE2 . TRP   A 1 265 ? -16.025 29.620  13.529  1.00 48.51  ? 262 TRP   A CE2 1 
ATOM   2006 C CE3 . TRP   A 1 265 ? -15.354 27.353  13.015  1.00 50.09  ? 262 TRP   A CE3 1 
ATOM   2007 C CZ2 . TRP   A 1 265 ? -14.985 29.766  14.439  1.00 53.82  ? 262 TRP   A CZ2 1 
ATOM   2008 C CZ3 . TRP   A 1 265 ? -14.334 27.497  13.920  1.00 55.34  ? 262 TRP   A CZ3 1 
ATOM   2009 C CH2 . TRP   A 1 265 ? -14.152 28.693  14.622  1.00 57.14  ? 262 TRP   A CH2 1 
ATOM   2010 N N   . ALA   A 1 266 ? -20.509 29.015  10.010  1.00 43.54  ? 263 ALA   A N   1 
ATOM   2011 C CA  . ALA   A 1 266 ? -21.259 30.258  9.915   1.00 46.39  ? 263 ALA   A CA  1 
ATOM   2012 C C   . ALA   A 1 266 ? -22.703 30.079  10.364  1.00 44.22  ? 263 ALA   A C   1 
ATOM   2013 O O   . ALA   A 1 266 ? -23.304 31.028  10.867  1.00 46.88  ? 263 ALA   A O   1 
ATOM   2014 C CB  . ALA   A 1 266 ? -21.191 30.803  8.489   1.00 43.05  ? 263 ALA   A CB  1 
ATOM   2015 N N   . THR   A 1 267 ? -23.283 28.891  10.188  1.00 41.30  ? 264 THR   A N   1 
ATOM   2016 C CA  . THR   A 1 267 ? -24.601 28.637  10.769  1.00 44.70  ? 264 THR   A CA  1 
ATOM   2017 C C   . THR   A 1 267 ? -24.489 28.273  12.256  1.00 47.37  ? 264 THR   A C   1 
ATOM   2018 O O   . THR   A 1 267 ? -25.021 28.976  13.118  1.00 47.29  ? 264 THR   A O   1 
ATOM   2019 C CB  . THR   A 1 267 ? -25.319 27.532  9.986   1.00 42.79  ? 264 THR   A CB  1 
ATOM   2020 O OG1 . THR   A 1 267 ? -25.510 27.949  8.632   1.00 48.91  ? 264 THR   A OG1 1 
ATOM   2021 C CG2 . THR   A 1 267 ? -26.673 27.221  10.601  1.00 43.80  ? 264 THR   A CG2 1 
ATOM   2022 N N   . GLN   A 1 268 ? -23.747 27.203  12.569  1.00 44.88  ? 265 GLN   A N   1 
ATOM   2023 C CA  . GLN   A 1 268 ? -23.647 26.689  13.936  1.00 43.48  ? 265 GLN   A CA  1 
ATOM   2024 C C   . GLN   A 1 268 ? -23.104 27.735  14.921  1.00 48.16  ? 265 GLN   A C   1 
ATOM   2025 O O   . GLN   A 1 268 ? -23.662 27.930  16.008  1.00 51.74  ? 265 GLN   A O   1 
ATOM   2026 C CB  . GLN   A 1 268 ? -22.765 25.439  13.925  1.00 46.15  ? 265 GLN   A CB  1 
ATOM   2027 C CG  . GLN   A 1 268 ? -22.397 24.905  15.288  1.00 52.83  ? 265 GLN   A CG  1 
ATOM   2028 C CD  . GLN   A 1 268 ? -23.610 24.398  16.030  1.00 60.60  ? 265 GLN   A CD  1 
ATOM   2029 O OE1 . GLN   A 1 268 ? -24.585 23.954  15.401  1.00 58.27  ? 265 GLN   A OE1 1 
ATOM   2030 N NE2 . GLN   A 1 268 ? -23.580 24.483  17.375  1.00 50.78  ? 265 GLN   A NE2 1 
ATOM   2031 N N   . VAL   A 1 269 ? -22.006 28.399  14.581  1.00 42.43  ? 266 VAL   A N   1 
ATOM   2032 C CA  . VAL   A 1 269 ? -21.407 29.354  15.510  1.00 45.57  ? 266 VAL   A CA  1 
ATOM   2033 C C   . VAL   A 1 269 ? -21.969 30.760  15.312  1.00 48.91  ? 266 VAL   A C   1 
ATOM   2034 O O   . VAL   A 1 269 ? -22.357 31.415  16.279  1.00 48.88  ? 266 VAL   A O   1 
ATOM   2035 C CB  . VAL   A 1 269 ? -19.867 29.337  15.382  1.00 48.16  ? 266 VAL   A CB  1 
ATOM   2036 C CG1 . VAL   A 1 269 ? -19.254 30.477  16.189  1.00 43.64  ? 266 VAL   A CG1 1 
ATOM   2037 C CG2 . VAL   A 1 269 ? -19.299 27.975  15.823  1.00 39.45  ? 266 VAL   A CG2 1 
ATOM   2038 N N   . GLN   A 1 270 ? -22.027 31.263  14.073  1.00 51.44  ? 267 GLN   A N   1 
ATOM   2039 C CA  . GLN   A 1 270 ? -22.456 32.639  13.807  1.00 47.02  ? 267 GLN   A CA  1 
ATOM   2040 C C   . GLN   A 1 270 ? -23.951 32.778  13.532  1.00 45.35  ? 267 GLN   A C   1 
ATOM   2041 O O   . GLN   A 1 270 ? -24.407 33.891  13.265  1.00 47.91  ? 267 GLN   A O   1 
ATOM   2042 C CB  . GLN   A 1 270 ? -21.687 33.233  12.622  1.00 46.89  ? 267 GLN   A CB  1 
ATOM   2043 C CG  . GLN   A 1 270 ? -20.246 33.614  12.903  1.00 54.78  ? 267 GLN   A CG  1 
ATOM   2044 C CD  . GLN   A 1 270 ? -19.484 33.925  11.617  1.00 60.04  ? 267 GLN   A CD  1 
ATOM   2045 O OE1 . GLN   A 1 270 ? -19.919 33.555  10.527  1.00 54.71  ? 267 GLN   A OE1 1 
ATOM   2046 N NE2 . GLN   A 1 270 ? -18.348 34.612  11.740  1.00 60.64  ? 267 GLN   A NE2 1 
ATOM   2047 N N   . ARG   A 1 271 ? -24.714 31.687  13.560  1.00 44.66  ? 268 ARG   A N   1 
ATOM   2048 C CA  . ARG   A 1 271 ? -26.179 31.741  13.517  1.00 50.12  ? 268 ARG   A CA  1 
ATOM   2049 C C   . ARG   A 1 271 ? -26.706 32.385  12.229  1.00 55.37  ? 268 ARG   A C   1 
ATOM   2050 O O   . ARG   A 1 271 ? -27.664 33.160  12.247  1.00 57.53  ? 268 ARG   A O   1 
ATOM   2051 C CB  . ARG   A 1 271 ? -26.718 32.448  14.760  1.00 55.32  ? 268 ARG   A CB  1 
ATOM   2052 C CG  . ARG   A 1 271 ? -25.928 32.093  16.025  1.00 56.82  ? 268 ARG   A CG  1 
ATOM   2053 C CD  . ARG   A 1 271 ? -26.674 32.404  17.309  1.00 62.20  ? 268 ARG   A CD  1 
ATOM   2054 N NE  . ARG   A 1 271 ? -27.812 31.514  17.527  1.00 69.84  ? 268 ARG   A NE  1 
ATOM   2055 C CZ  . ARG   A 1 271 ? -29.087 31.861  17.383  1.00 70.09  ? 268 ARG   A CZ  1 
ATOM   2056 N NH1 . ARG   A 1 271 ? -29.434 33.085  16.999  1.00 64.06  ? 268 ARG   A NH1 1 
ATOM   2057 N NH2 . ARG   A 1 271 ? -30.038 30.962  17.648  1.00 59.89  ? 268 ARG   A NH2 1 
ATOM   2058 N N   . ASP   A 1 272 ? -26.082 32.035  11.097  1.00 54.02  ? 269 ASP   A N   1 
ATOM   2059 C CA  . ASP   A 1 272 ? -26.479 32.467  9.754   1.00 47.66  ? 269 ASP   A CA  1 
ATOM   2060 C C   . ASP   A 1 272 ? -27.443 31.413  9.211   1.00 48.60  ? 269 ASP   A C   1 
ATOM   2061 O O   . ASP   A 1 272 ? -27.038 30.427  8.595   1.00 52.86  ? 269 ASP   A O   1 
ATOM   2062 C CB  . ASP   A 1 272 ? -25.227 32.634  8.894   1.00 52.54  ? 269 ASP   A CB  1 
ATOM   2063 C CG  . ASP   A 1 272 ? -25.485 33.314  7.540   1.00 59.15  ? 269 ASP   A CG  1 
ATOM   2064 O OD1 . ASP   A 1 272 ? -26.313 32.822  6.739   1.00 58.92  ? 269 ASP   A OD1 1 
ATOM   2065 O OD2 . ASP   A 1 272 ? -24.815 34.335  7.262   1.00 61.47  ? 269 ASP   A OD2 1 
ATOM   2066 N N   . TYR   A 1 273 ? -28.740 31.605  9.446   1.00 48.38  ? 270 TYR   A N   1 
ATOM   2067 C CA  . TYR   A 1 273 ? -29.695 30.520  9.220   1.00 51.14  ? 270 TYR   A CA  1 
ATOM   2068 C C   . TYR   A 1 273 ? -30.358 30.565  7.855   1.00 52.85  ? 270 TYR   A C   1 
ATOM   2069 O O   . TYR   A 1 273 ? -30.803 29.525  7.352   1.00 51.11  ? 270 TYR   A O   1 
ATOM   2070 C CB  . TYR   A 1 273 ? -30.791 30.531  10.293  1.00 50.83  ? 270 TYR   A CB  1 
ATOM   2071 C CG  . TYR   A 1 273 ? -30.275 30.161  11.667  1.00 60.35  ? 270 TYR   A CG  1 
ATOM   2072 C CD1 . TYR   A 1 273 ? -29.744 28.892  11.913  1.00 60.64  ? 270 TYR   A CD1 1 
ATOM   2073 C CD2 . TYR   A 1 273 ? -30.306 31.077  12.717  1.00 58.15  ? 270 TYR   A CD2 1 
ATOM   2074 C CE1 . TYR   A 1 273 ? -29.253 28.548  13.162  1.00 58.33  ? 270 TYR   A CE1 1 
ATOM   2075 C CE2 . TYR   A 1 273 ? -29.823 30.740  13.967  1.00 65.06  ? 270 TYR   A CE2 1 
ATOM   2076 C CZ  . TYR   A 1 273 ? -29.299 29.476  14.184  1.00 63.64  ? 270 TYR   A CZ  1 
ATOM   2077 O OH  . TYR   A 1 273 ? -28.821 29.147  15.431  1.00 67.39  ? 270 TYR   A OH  1 
ATOM   2078 N N   . HIS   A 1 274 ? -30.458 31.740  7.255   1.00 51.87  ? 271 HIS   A N   1 
ATOM   2079 C CA  . HIS   A 1 274 ? -31.128 31.887  5.981   1.00 50.35  ? 271 HIS   A CA  1 
ATOM   2080 C C   . HIS   A 1 274 ? -30.155 32.463  4.972   1.00 50.28  ? 271 HIS   A C   1 
ATOM   2081 O O   . HIS   A 1 274 ? -29.178 33.133  5.329   1.00 51.70  ? 271 HIS   A O   1 
ATOM   2082 C CB  . HIS   A 1 274 ? -32.373 32.766  6.112   1.00 48.19  ? 271 HIS   A CB  1 
ATOM   2083 C CG  . HIS   A 1 274 ? -33.473 32.107  6.881   1.00 56.14  ? 271 HIS   A CG  1 
ATOM   2084 N ND1 . HIS   A 1 274 ? -33.469 32.017  8.258   1.00 62.52  ? 271 HIS   A ND1 1 
ATOM   2085 C CD2 . HIS   A 1 274 ? -34.595 31.469  6.467   1.00 58.35  ? 271 HIS   A CD2 1 
ATOM   2086 C CE1 . HIS   A 1 274 ? -34.548 31.367  8.659   1.00 59.65  ? 271 HIS   A CE1 1 
ATOM   2087 N NE2 . HIS   A 1 274 ? -35.248 31.023  7.592   1.00 59.70  ? 271 HIS   A NE2 1 
ATOM   2088 N N   . GLY   A 1 275 ? -30.424 32.172  3.705   1.00 46.16  ? 272 GLY   A N   1 
ATOM   2089 C CA  . GLY   A 1 275 ? -29.609 32.685  2.631   1.00 47.23  ? 272 GLY   A CA  1 
ATOM   2090 C C   . GLY   A 1 275 ? -30.103 32.234  1.279   1.00 45.79  ? 272 GLY   A C   1 
ATOM   2091 O O   . GLY   A 1 275 ? -31.114 31.531  1.160   1.00 41.96  ? 272 GLY   A O   1 
ATOM   2092 N N   . PRO   A 1 276 ? -29.398 32.637  0.225   1.00 49.37  ? 273 PRO   A N   1 
ATOM   2093 C CA  . PRO   A 1 276 ? -29.858 32.309  -1.130  1.00 43.97  ? 273 PRO   A CA  1 
ATOM   2094 C C   . PRO   A 1 276 ? -29.948 30.803  -1.316  1.00 40.15  ? 273 PRO   A C   1 
ATOM   2095 O O   . PRO   A 1 276 ? -29.051 30.059  -0.911  1.00 42.89  ? 273 PRO   A O   1 
ATOM   2096 C CB  . PRO   A 1 276 ? -28.789 32.939  -2.028  1.00 40.70  ? 273 PRO   A CB  1 
ATOM   2097 C CG  . PRO   A 1 276 ? -27.575 33.097  -1.140  1.00 43.36  ? 273 PRO   A CG  1 
ATOM   2098 C CD  . PRO   A 1 276 ? -28.118 33.367  0.227   1.00 44.09  ? 273 PRO   A CD  1 
ATOM   2099 N N   . ARG   A 1 277 ? -31.057 30.353  -1.897  1.00 34.18  ? 274 ARG   A N   1 
ATOM   2100 C CA  . ARG   A 1 277 ? -31.227 28.933  -2.152  1.00 37.69  ? 274 ARG   A CA  1 
ATOM   2101 C C   . ARG   A 1 277 ? -30.111 28.434  -3.058  1.00 41.24  ? 274 ARG   A C   1 
ATOM   2102 O O   . ARG   A 1 277 ? -29.898 28.980  -4.143  1.00 40.32  ? 274 ARG   A O   1 
ATOM   2103 C CB  . ARG   A 1 277 ? -32.587 28.673  -2.784  1.00 37.49  ? 274 ARG   A CB  1 
ATOM   2104 C CG  . ARG   A 1 277 ? -33.714 29.339  -2.017  1.00 43.27  ? 274 ARG   A CG  1 
ATOM   2105 C CD  . ARG   A 1 277 ? -35.071 28.844  -2.437  1.00 45.04  ? 274 ARG   A CD  1 
ATOM   2106 N NE  . ARG   A 1 277 ? -36.045 29.148  -1.398  1.00 51.21  ? 274 ARG   A NE  1 
ATOM   2107 C CZ  . ARG   A 1 277 ? -36.439 28.282  -0.474  1.00 53.89  ? 274 ARG   A CZ  1 
ATOM   2108 N NH1 . ARG   A 1 277 ? -35.985 27.037  -0.453  1.00 56.92  ? 274 ARG   A NH1 1 
ATOM   2109 N NH2 . ARG   A 1 277 ? -37.316 28.668  0.447   1.00 54.74  ? 274 ARG   A NH2 1 
ATOM   2110 N N   . LEU   A 1 278 ? -29.385 27.408  -2.606  1.00 40.16  ? 275 LEU   A N   1 
ATOM   2111 C CA  . LEU   A 1 278 ? -28.242 26.924  -3.364  1.00 39.11  ? 275 LEU   A CA  1 
ATOM   2112 C C   . LEU   A 1 278 ? -28.603 25.865  -4.402  1.00 38.90  ? 275 LEU   A C   1 
ATOM   2113 O O   . LEU   A 1 278 ? -27.954 25.806  -5.458  1.00 38.48  ? 275 LEU   A O   1 
ATOM   2114 C CB  . LEU   A 1 278 ? -27.173 26.371  -2.419  1.00 38.86  ? 275 LEU   A CB  1 
ATOM   2115 C CG  . LEU   A 1 278 ? -26.534 27.443  -1.527  1.00 40.20  ? 275 LEU   A CG  1 
ATOM   2116 C CD1 . LEU   A 1 278 ? -25.361 26.864  -0.739  1.00 38.58  ? 275 LEU   A CD1 1 
ATOM   2117 C CD2 . LEU   A 1 278 ? -26.108 28.666  -2.341  1.00 32.72  ? 275 LEU   A CD2 1 
ATOM   2118 N N   . LEU   A 1 279 ? -29.628 25.047  -4.151  1.00 36.18  ? 276 LEU   A N   1 
ATOM   2119 C CA  . LEU   A 1 279 ? -29.952 23.969  -5.084  1.00 36.08  ? 276 LEU   A CA  1 
ATOM   2120 C C   . LEU   A 1 279 ? -30.232 24.417  -6.525  1.00 41.45  ? 276 LEU   A C   1 
ATOM   2121 O O   . LEU   A 1 279 ? -29.935 23.628  -7.444  1.00 38.89  ? 276 LEU   A O   1 
ATOM   2122 C CB  . LEU   A 1 279 ? -31.122 23.154  -4.530  1.00 29.55  ? 276 LEU   A CB  1 
ATOM   2123 C CG  . LEU   A 1 279 ? -30.819 22.369  -3.247  1.00 37.99  ? 276 LEU   A CG  1 
ATOM   2124 C CD1 . LEU   A 1 279 ? -31.890 21.330  -3.016  1.00 36.28  ? 276 LEU   A CD1 1 
ATOM   2125 C CD2 . LEU   A 1 279 ? -29.453 21.708  -3.306  1.00 35.10  ? 276 LEU   A CD2 1 
ATOM   2126 N N   . PRO   A 1 280 ? -30.786 25.607  -6.803  1.00 40.98  ? 277 PRO   A N   1 
ATOM   2127 C CA  . PRO   A 1 280 ? -30.936 26.036  -8.215  1.00 39.29  ? 277 PRO   A CA  1 
ATOM   2128 C C   . PRO   A 1 280 ? -29.623 26.100  -9.003  1.00 42.38  ? 277 PRO   A C   1 
ATOM   2129 O O   . PRO   A 1 280 ? -29.671 26.191  -10.239 1.00 41.82  ? 277 PRO   A O   1 
ATOM   2130 C CB  . PRO   A 1 280 ? -31.564 27.429  -8.089  1.00 37.54  ? 277 PRO   A CB  1 
ATOM   2131 C CG  . PRO   A 1 280 ? -32.363 27.352  -6.840  1.00 42.24  ? 277 PRO   A CG  1 
ATOM   2132 C CD  . PRO   A 1 280 ? -31.568 26.474  -5.896  1.00 40.68  ? 277 PRO   A CD  1 
ATOM   2133 N N   . TYR   A 1 281 ? -28.469 26.070  -8.333  1.00 35.92  ? 278 TYR   A N   1 
ATOM   2134 C CA  . TYR   A 1 281 ? -27.184 26.248  -8.983  1.00 33.70  ? 278 TYR   A CA  1 
ATOM   2135 C C   . TYR   A 1 281 ? -26.456 24.937  -9.258  1.00 33.85  ? 278 TYR   A C   1 
ATOM   2136 O O   . TYR   A 1 281 ? -25.316 24.966  -9.733  1.00 37.02  ? 278 TYR   A O   1 
ATOM   2137 C CB  . TYR   A 1 281 ? -26.296 27.154  -8.127  1.00 37.19  ? 278 TYR   A CB  1 
ATOM   2138 C CG  . TYR   A 1 281 ? -26.804 28.568  -8.020  1.00 40.84  ? 278 TYR   A CG  1 
ATOM   2139 C CD1 . TYR   A 1 281 ? -27.874 28.884  -7.196  1.00 40.04  ? 278 TYR   A CD1 1 
ATOM   2140 C CD2 . TYR   A 1 281 ? -26.203 29.600  -8.735  1.00 43.24  ? 278 TYR   A CD2 1 
ATOM   2141 C CE1 . TYR   A 1 281 ? -28.349 30.188  -7.096  1.00 41.99  ? 278 TYR   A CE1 1 
ATOM   2142 C CE2 . TYR   A 1 281 ? -26.665 30.918  -8.632  1.00 46.29  ? 278 TYR   A CE2 1 
ATOM   2143 C CZ  . TYR   A 1 281 ? -27.744 31.201  -7.813  1.00 50.42  ? 278 TYR   A CZ  1 
ATOM   2144 O OH  . TYR   A 1 281 ? -28.215 32.496  -7.704  1.00 48.92  ? 278 TYR   A OH  1 
ATOM   2145 N N   . ILE   A 1 282 ? -27.058 23.790  -8.957  1.00 31.86  ? 279 ILE   A N   1 
ATOM   2146 C CA  . ILE   A 1 282 ? -26.338 22.521  -9.044  1.00 33.91  ? 279 ILE   A CA  1 
ATOM   2147 C C   . ILE   A 1 282 ? -26.833 21.652  -10.172 1.00 32.68  ? 279 ILE   A C   1 
ATOM   2148 O O   . ILE   A 1 282 ? -26.214 20.608  -10.439 1.00 35.83  ? 279 ILE   A O   1 
ATOM   2149 C CB  . ILE   A 1 282 ? -26.381 21.723  -7.717  1.00 33.44  ? 279 ILE   A CB  1 
ATOM   2150 C CG1 . ILE   A 1 282 ? -27.755 21.057  -7.518  1.00 29.82  ? 279 ILE   A CG1 1 
ATOM   2151 C CG2 . ILE   A 1 282 ? -25.982 22.606  -6.512  1.00 28.99  ? 279 ILE   A CG2 1 
ATOM   2152 C CD1 . ILE   A 1 282 ? -27.767 19.956  -6.501  1.00 33.10  ? 279 ILE   A CD1 1 
ATOM   2153 N N   . MET   A 1 283 ? -27.909 22.044  -10.855 1.00 30.22  ? 280 MET   A N   1 
ATOM   2154 C CA  . MET   A 1 283 ? -28.490 21.179  -11.876 1.00 31.35  ? 280 MET   A CA  1 
ATOM   2155 C C   . MET   A 1 283 ? -27.629 21.137  -13.135 1.00 34.81  ? 280 MET   A C   1 
ATOM   2156 O O   . MET   A 1 283 ? -27.152 20.065  -13.537 1.00 31.71  ? 280 MET   A O   1 
ATOM   2157 C CB  . MET   A 1 283 ? -29.909 21.629  -12.190 1.00 35.23  ? 280 MET   A CB  1 
ATOM   2158 C CG  . MET   A 1 283 ? -30.913 21.149  -11.163 1.00 37.25  ? 280 MET   A CG  1 
ATOM   2159 S SD  . MET   A 1 283 ? -32.501 21.957  -11.402 1.00 42.55  ? 280 MET   A SD  1 
ATOM   2160 C CE  . MET   A 1 283 ? -32.108 23.670  -11.035 1.00 32.33  ? 280 MET   A CE  1 
ATOM   2161 N N   . PHE   A 1 284 ? -27.422 22.288  -13.785 1.00 33.22  ? 281 PHE   A N   1 
ATOM   2162 C CA  . PHE   A 1 284 ? -26.557 22.273  -14.961 1.00 33.52  ? 281 PHE   A CA  1 
ATOM   2163 C C   . PHE   A 1 284 ? -25.151 21.778  -14.650 1.00 29.90  ? 281 PHE   A C   1 
ATOM   2164 O O   . PHE   A 1 284 ? -24.646 20.939  -15.415 1.00 33.39  ? 281 PHE   A O   1 
ATOM   2165 C CB  . PHE   A 1 284 ? -26.480 23.638  -15.654 1.00 34.64  ? 281 PHE   A CB  1 
ATOM   2166 C CG  . PHE   A 1 284 ? -25.543 23.621  -16.826 1.00 38.48  ? 281 PHE   A CG  1 
ATOM   2167 C CD1 . PHE   A 1 284 ? -25.925 23.017  -18.025 1.00 32.54  ? 281 PHE   A CD1 1 
ATOM   2168 C CD2 . PHE   A 1 284 ? -24.251 24.125  -16.719 1.00 35.50  ? 281 PHE   A CD2 1 
ATOM   2169 C CE1 . PHE   A 1 284 ? -25.044 22.955  -19.093 1.00 32.22  ? 281 PHE   A CE1 1 
ATOM   2170 C CE2 . PHE   A 1 284 ? -23.371 24.061  -17.803 1.00 33.04  ? 281 PHE   A CE2 1 
ATOM   2171 C CZ  . PHE   A 1 284 ? -23.770 23.475  -18.976 1.00 31.79  ? 281 PHE   A CZ  1 
ATOM   2172 N N   . PRO   A 1 285 ? -24.476 22.218  -13.583 1.00 31.24  ? 282 PRO   A N   1 
ATOM   2173 C CA  . PRO   A 1 285 ? -23.178 21.599  -13.237 1.00 31.30  ? 282 PRO   A CA  1 
ATOM   2174 C C   . PRO   A 1 285 ? -23.258 20.112  -12.946 1.00 32.99  ? 282 PRO   A C   1 
ATOM   2175 O O   . PRO   A 1 285 ? -22.206 19.460  -12.921 1.00 35.41  ? 282 PRO   A O   1 
ATOM   2176 C CB  . PRO   A 1 285 ? -22.735 22.367  -11.983 1.00 29.70  ? 282 PRO   A CB  1 
ATOM   2177 C CG  . PRO   A 1 285 ? -23.447 23.687  -12.078 1.00 35.00  ? 282 PRO   A CG  1 
ATOM   2178 C CD  . PRO   A 1 285 ? -24.771 23.385  -12.725 1.00 33.20  ? 282 PRO   A CD  1 
ATOM   2179 N N   . ARG   A 1 286 ? -24.450 19.560  -12.710 1.00 29.28  ? 283 ARG   A N   1 
ATOM   2180 C CA  . ARG   A 1 286 ? -24.577 18.180  -12.268 1.00 31.41  ? 283 ARG   A CA  1 
ATOM   2181 C C   . ARG   A 1 286 ? -23.671 17.915  -11.063 1.00 29.65  ? 283 ARG   A C   1 
ATOM   2182 O O   . ARG   A 1 286 ? -22.940 16.924  -11.007 1.00 30.50  ? 283 ARG   A O   1 
ATOM   2183 C CB  . ARG   A 1 286 ? -24.261 17.217  -13.413 1.00 31.14  ? 283 ARG   A CB  1 
ATOM   2184 C CG  . ARG   A 1 286 ? -25.329 17.081  -14.486 1.00 34.11  ? 283 ARG   A CG  1 
ATOM   2185 C CD  . ARG   A 1 286 ? -24.700 16.997  -15.879 1.00 28.73  ? 283 ARG   A CD  1 
ATOM   2186 N NE  . ARG   A 1 286 ? -24.466 18.339  -16.397 1.00 31.80  ? 283 ARG   A NE  1 
ATOM   2187 C CZ  . ARG   A 1 286 ? -23.807 18.616  -17.513 1.00 33.06  ? 283 ARG   A CZ  1 
ATOM   2188 N NH1 . ARG   A 1 286 ? -23.210 17.671  -18.217 1.00 31.35  ? 283 ARG   A NH1 1 
ATOM   2189 N NH2 . ARG   A 1 286 ? -23.755 19.871  -17.941 1.00 34.64  ? 283 ARG   A NH2 1 
ATOM   2190 N N   . ALA   A 1 287 ? -23.701 18.836  -10.106 1.00 27.19  ? 284 ALA   A N   1 
ATOM   2191 C CA  . ALA   A 1 287 ? -22.831 18.749  -8.942  1.00 30.37  ? 284 ALA   A CA  1 
ATOM   2192 C C   . ALA   A 1 287 ? -23.390 17.756  -7.944  1.00 32.89  ? 284 ALA   A C   1 
ATOM   2193 O O   . ALA   A 1 287 ? -24.608 17.586  -7.821  1.00 32.16  ? 284 ALA   A O   1 
ATOM   2194 C CB  . ALA   A 1 287 ? -22.660 20.111  -8.259  1.00 27.55  ? 284 ALA   A CB  1 
ATOM   2195 N N   . THR   A 1 288 ? -22.479 17.093  -7.235  1.00 32.42  ? 285 THR   A N   1 
ATOM   2196 C CA  . THR   A 1 288 ? -22.807 16.126  -6.194  1.00 29.73  ? 285 THR   A CA  1 
ATOM   2197 C C   . THR   A 1 288 ? -22.377 16.710  -4.859  1.00 31.62  ? 285 THR   A C   1 
ATOM   2198 O O   . THR   A 1 288 ? -21.230 17.144  -4.716  1.00 30.41  ? 285 THR   A O   1 
ATOM   2199 C CB  . THR   A 1 288 ? -22.091 14.788  -6.441  1.00 32.94  ? 285 THR   A CB  1 
ATOM   2200 O OG1 . THR   A 1 288 ? -22.383 14.318  -7.763  1.00 33.64  ? 285 THR   A OG1 1 
ATOM   2201 C CG2 . THR   A 1 288 ? -22.511 13.734  -5.419  1.00 31.77  ? 285 THR   A CG2 1 
ATOM   2202 N N   . ILE   A 1 289 ? -23.289 16.733  -3.894  1.00 30.64  ? 286 ILE   A N   1 
ATOM   2203 C CA  . ILE   A 1 289 ? -23.014 17.250  -2.558  1.00 28.50  ? 286 ILE   A CA  1 
ATOM   2204 C C   . ILE   A 1 289 ? -23.213 16.111  -1.570  1.00 29.82  ? 286 ILE   A C   1 
ATOM   2205 O O   . ILE   A 1 289 ? -24.294 15.513  -1.527  1.00 32.68  ? 286 ILE   A O   1 
ATOM   2206 C CB  . ILE   A 1 289 ? -23.922 18.443  -2.211  1.00 29.08  ? 286 ILE   A CB  1 
ATOM   2207 C CG1 . ILE   A 1 289 ? -23.781 19.540  -3.259  1.00 32.79  ? 286 ILE   A CG1 1 
ATOM   2208 C CG2 . ILE   A 1 289 ? -23.554 19.036  -0.866  1.00 29.56  ? 286 ILE   A CG2 1 
ATOM   2209 C CD1 . ILE   A 1 289 ? -24.789 19.455  -4.382  1.00 36.18  ? 286 ILE   A CD1 1 
ATOM   2210 N N   . ARG   A 1 290 ? -22.186 15.808  -0.773  1.00 29.39  ? 287 ARG   A N   1 
ATOM   2211 C CA  . ARG   A 1 290 ? -22.286 14.751  0.229   1.00 30.16  ? 287 ARG   A CA  1 
ATOM   2212 C C   . ARG   A 1 290 ? -22.026 15.290  1.630   1.00 31.31  ? 287 ARG   A C   1 
ATOM   2213 O O   . ARG   A 1 290 ? -20.980 15.889  1.898   1.00 33.02  ? 287 ARG   A O   1 
ATOM   2214 C CB  . ARG   A 1 290 ? -21.332 13.591  -0.064  1.00 32.84  ? 287 ARG   A CB  1 
ATOM   2215 C CG  . ARG   A 1 290 ? -21.713 12.324  0.758   1.00 35.51  ? 287 ARG   A CG  1 
ATOM   2216 C CD  . ARG   A 1 290 ? -20.748 11.206  0.518   1.00 32.19  ? 287 ARG   A CD  1 
ATOM   2217 N NE  . ARG   A 1 290 ? -21.042 9.976   1.248   1.00 41.31  ? 287 ARG   A NE  1 
ATOM   2218 C CZ  . ARG   A 1 290 ? -20.819 9.769   2.545   1.00 36.42  ? 287 ARG   A CZ  1 
ATOM   2219 N NH1 . ARG   A 1 290 ? -20.539 10.767  3.377   1.00 36.55  ? 287 ARG   A NH1 1 
ATOM   2220 N NH2 . ARG   A 1 290 ? -20.877 8.529   3.020   1.00 35.63  ? 287 ARG   A NH2 1 
ATOM   2221 N N   . GLY   A 1 291 ? -22.982 15.070  2.525   1.00 33.64  ? 288 GLY   A N   1 
ATOM   2222 C CA  . GLY   A 1 291 ? -22.727 15.299  3.934   1.00 31.29  ? 288 GLY   A CA  1 
ATOM   2223 C C   . GLY   A 1 291 ? -21.654 14.361  4.468   1.00 29.58  ? 288 GLY   A C   1 
ATOM   2224 O O   . GLY   A 1 291 ? -21.619 13.166  4.155   1.00 27.66  ? 288 GLY   A O   1 
ATOM   2225 N N   . ILE   A 1 292 ? -20.765 14.919  5.286   1.00 27.72  ? 289 ILE   A N   1 
ATOM   2226 C CA  . ILE   A 1 292 ? -19.716 14.150  5.945   1.00 33.24  ? 289 ILE   A CA  1 
ATOM   2227 C C   . ILE   A 1 292 ? -20.088 13.935  7.409   1.00 34.76  ? 289 ILE   A C   1 
ATOM   2228 O O   . ILE   A 1 292 ? -20.394 14.891  8.138   1.00 33.98  ? 289 ILE   A O   1 
ATOM   2229 C CB  . ILE   A 1 292 ? -18.349 14.840  5.830   1.00 31.63  ? 289 ILE   A CB  1 
ATOM   2230 C CG1 . ILE   A 1 292 ? -18.051 15.182  4.365   1.00 27.38  ? 289 ILE   A CG1 1 
ATOM   2231 C CG2 . ILE   A 1 292 ? -17.274 13.931  6.424   1.00 26.06  ? 289 ILE   A CG2 1 
ATOM   2232 C CD1 . ILE   A 1 292 ? -18.328 13.993  3.409   1.00 27.15  ? 289 ILE   A CD1 1 
ATOM   2233 N N   . PHE   A 1 293 ? -20.067 12.674  7.839   1.00 33.05  ? 290 PHE   A N   1 
ATOM   2234 C CA  . PHE   A 1 293 ? -20.175 12.319  9.262   1.00 36.03  ? 290 PHE   A CA  1 
ATOM   2235 C C   . PHE   A 1 293 ? -19.177 11.181  9.458   1.00 33.26  ? 290 PHE   A C   1 
ATOM   2236 O O   . PHE   A 1 293 ? -19.536 10.001  9.358   1.00 30.92  ? 290 PHE   A O   1 
ATOM   2237 C CB  . PHE   A 1 293 ? -21.597 11.916  9.658   1.00 36.37  ? 290 PHE   A CB  1 
ATOM   2238 C CG  . PHE   A 1 293 ? -21.838 11.919  11.142  1.00 38.38  ? 290 PHE   A CG  1 
ATOM   2239 C CD1 . PHE   A 1 293 ? -21.839 13.112  11.851  1.00 38.01  ? 290 PHE   A CD1 1 
ATOM   2240 C CD2 . PHE   A 1 293 ? -22.068 10.732  11.829  1.00 39.12  ? 290 PHE   A CD2 1 
ATOM   2241 C CE1 . PHE   A 1 293 ? -22.039 13.116  13.221  1.00 41.60  ? 290 PHE   A CE1 1 
ATOM   2242 C CE2 . PHE   A 1 293 ? -22.284 10.730  13.201  1.00 39.16  ? 290 PHE   A CE2 1 
ATOM   2243 C CZ  . PHE   A 1 293 ? -22.261 11.925  13.896  1.00 41.55  ? 290 PHE   A CZ  1 
ATOM   2244 N N   . SER   A 1 294 ? -17.916 11.542  9.713   1.00 28.22  ? 291 SER   A N   1 
ATOM   2245 C CA  . SER   A 1 294 ? -16.833 10.568  9.613   1.00 31.11  ? 291 SER   A CA  1 
ATOM   2246 C C   . SER   A 1 294 ? -16.911 9.434   10.641  1.00 32.48  ? 291 SER   A C   1 
ATOM   2247 O O   . SER   A 1 294 ? -16.204 8.431   10.471  1.00 30.58  ? 291 SER   A O   1 
ATOM   2248 C CB  . SER   A 1 294 ? -15.509 11.288  9.747   1.00 31.26  ? 291 SER   A CB  1 
ATOM   2249 O OG  . SER   A 1 294 ? -15.505 12.007  10.958  1.00 40.29  ? 291 SER   A OG  1 
ATOM   2250 N N   . LEU   A 1 295 ? -17.743 9.556   11.685  1.00 30.70  ? 292 LEU   A N   1 
ATOM   2251 C CA  . LEU   A 1 295 ? -17.991 8.424   12.579  1.00 31.57  ? 292 LEU   A CA  1 
ATOM   2252 C C   . LEU   A 1 295 ? -18.310 7.141   11.819  1.00 36.90  ? 292 LEU   A C   1 
ATOM   2253 O O   . LEU   A 1 295 ? -17.932 6.051   12.264  1.00 34.97  ? 292 LEU   A O   1 
ATOM   2254 C CB  . LEU   A 1 295 ? -19.133 8.740   13.532  1.00 28.21  ? 292 LEU   A CB  1 
ATOM   2255 C CG  . LEU   A 1 295 ? -18.705 9.520   14.762  1.00 36.80  ? 292 LEU   A CG  1 
ATOM   2256 C CD1 . LEU   A 1 295 ? -19.752 9.434   15.873  1.00 39.58  ? 292 LEU   A CD1 1 
ATOM   2257 C CD2 . LEU   A 1 295 ? -17.313 9.056   15.231  1.00 33.66  ? 292 LEU   A CD2 1 
ATOM   2258 N N   . GLU   A 1 296 ? -18.985 7.254   10.664  1.00 34.21  ? 293 GLU   A N   1 
ATOM   2259 C CA  . GLU   A 1 296 ? -19.372 6.081   9.886   1.00 30.34  ? 293 GLU   A CA  1 
ATOM   2260 C C   . GLU   A 1 296 ? -18.173 5.307   9.385   1.00 31.70  ? 293 GLU   A C   1 
ATOM   2261 O O   . GLU   A 1 296 ? -18.336 4.150   8.983   1.00 32.09  ? 293 GLU   A O   1 
ATOM   2262 C CB  . GLU   A 1 296 ? -20.249 6.474   8.680   1.00 33.64  ? 293 GLU   A CB  1 
ATOM   2263 C CG  . GLU   A 1 296 ? -19.479 7.093   7.509   1.00 33.26  ? 293 GLU   A CG  1 
ATOM   2264 C CD  . GLU   A 1 296 ? -20.268 7.121   6.182   1.00 39.69  ? 293 GLU   A CD  1 
ATOM   2265 O OE1 . GLU   A 1 296 ? -20.988 6.139   5.881   1.00 39.31  ? 293 GLU   A OE1 1 
ATOM   2266 O OE2 . GLU   A 1 296 ? -20.154 8.126   5.432   1.00 31.52  ? 293 GLU   A OE2 1 
ATOM   2267 N N   . TRP   A 1 297 ? -16.983 5.919   9.377   1.00 32.95  ? 294 TRP   A N   1 
ATOM   2268 C CA  . TRP   A 1 297 ? -15.767 5.269   8.900   1.00 32.08  ? 294 TRP   A CA  1 
ATOM   2269 C C   . TRP   A 1 297 ? -14.896 4.726   10.033  1.00 34.34  ? 294 TRP   A C   1 
ATOM   2270 O O   . TRP   A 1 297 ? -13.809 4.212   9.768   1.00 36.81  ? 294 TRP   A O   1 
ATOM   2271 C CB  . TRP   A 1 297 ? -14.943 6.233   8.039   1.00 29.55  ? 294 TRP   A CB  1 
ATOM   2272 C CG  . TRP   A 1 297 ? -15.642 6.712   6.799   1.00 36.32  ? 294 TRP   A CG  1 
ATOM   2273 C CD1 . TRP   A 1 297 ? -16.450 5.980   5.958   1.00 35.99  ? 294 TRP   A CD1 1 
ATOM   2274 C CD2 . TRP   A 1 297 ? -15.611 8.038   6.262   1.00 30.74  ? 294 TRP   A CD2 1 
ATOM   2275 N NE1 . TRP   A 1 297 ? -16.909 6.773   4.931   1.00 31.72  ? 294 TRP   A NE1 1 
ATOM   2276 C CE2 . TRP   A 1 297 ? -16.410 8.042   5.100   1.00 34.68  ? 294 TRP   A CE2 1 
ATOM   2277 C CE3 . TRP   A 1 297 ? -14.974 9.227   6.645   1.00 34.32  ? 294 TRP   A CE3 1 
ATOM   2278 C CZ2 . TRP   A 1 297 ? -16.599 9.200   4.323   1.00 35.92  ? 294 TRP   A CZ2 1 
ATOM   2279 C CZ3 . TRP   A 1 297 ? -15.153 10.377  5.860   1.00 28.60  ? 294 TRP   A CZ3 1 
ATOM   2280 C CH2 . TRP   A 1 297 ? -15.966 10.353  4.723   1.00 28.15  ? 294 TRP   A CH2 1 
ATOM   2281 N N   . PHE   A 1 298 ? -15.333 4.837   11.285  1.00 33.66  ? 295 PHE   A N   1 
ATOM   2282 C CA  . PHE   A 1 298 ? -14.575 4.312   12.420  1.00 32.05  ? 295 PHE   A CA  1 
ATOM   2283 C C   . PHE   A 1 298 ? -14.748 2.793   12.433  1.00 32.80  ? 295 PHE   A C   1 
ATOM   2284 O O   . PHE   A 1 298 ? -15.597 2.227   13.126  1.00 35.41  ? 295 PHE   A O   1 
ATOM   2285 C CB  . PHE   A 1 298 ? -15.052 4.940   13.727  1.00 34.67  ? 295 PHE   A CB  1 
ATOM   2286 C CG  . PHE   A 1 298 ? -14.578 6.357   13.959  1.00 34.52  ? 295 PHE   A CG  1 
ATOM   2287 C CD1 . PHE   A 1 298 ? -14.484 7.265   12.916  1.00 31.84  ? 295 PHE   A CD1 1 
ATOM   2288 C CD2 . PHE   A 1 298 ? -14.272 6.792   15.248  1.00 31.69  ? 295 PHE   A CD2 1 
ATOM   2289 C CE1 . PHE   A 1 298 ? -14.058 8.580   13.144  1.00 29.56  ? 295 PHE   A CE1 1 
ATOM   2290 C CE2 . PHE   A 1 298 ? -13.850 8.096   15.474  1.00 35.05  ? 295 PHE   A CE2 1 
ATOM   2291 C CZ  . PHE   A 1 298 ? -13.745 8.992   14.410  1.00 30.13  ? 295 PHE   A CZ  1 
ATOM   2292 N N   . THR   A 1 299 ? -13.935 2.130   11.628  1.00 30.66  ? 296 THR   A N   1 
ATOM   2293 C CA  . THR   A 1 299 ? -13.890 0.680   11.529  1.00 35.06  ? 296 THR   A CA  1 
ATOM   2294 C C   . THR   A 1 299 ? -12.436 0.262   11.653  1.00 39.51  ? 296 THR   A C   1 
ATOM   2295 O O   . THR   A 1 299 ? -11.531 1.031   11.324  1.00 42.57  ? 296 THR   A O   1 
ATOM   2296 C CB  . THR   A 1 299 ? -14.447 0.158   10.181  1.00 43.64  ? 296 THR   A CB  1 
ATOM   2297 O OG1 . THR   A 1 299 ? -13.629 0.629   9.090   1.00 38.38  ? 296 THR   A OG1 1 
ATOM   2298 C CG2 . THR   A 1 299 ? -15.897 0.587   9.963   1.00 32.00  ? 296 THR   A CG2 1 
ATOM   2299 N N   . GLU   A 1 300 ? -12.208 -0.970  12.108  1.00 44.08  ? 297 GLU   A N   1 
ATOM   2300 C CA  . GLU   A 1 300 ? -10.833 -1.440  12.260  1.00 42.53  ? 297 GLU   A CA  1 
ATOM   2301 C C   . GLU   A 1 300 ? -10.083 -1.401  10.932  1.00 39.72  ? 297 GLU   A C   1 
ATOM   2302 O O   . GLU   A 1 300 ? -8.912  -1.012  10.884  1.00 40.27  ? 297 GLU   A O   1 
ATOM   2303 C CB  . GLU   A 1 300 ? -10.827 -2.846  12.861  1.00 45.54  ? 297 GLU   A CB  1 
ATOM   2304 C CG  . GLU   A 1 300 ? -9.478  -3.556  12.854  1.00 55.18  ? 297 GLU   A CG  1 
ATOM   2305 C CD  . GLU   A 1 300 ? -9.414  -4.695  11.827  1.00 74.45  ? 297 GLU   A CD  1 
ATOM   2306 O OE1 . GLU   A 1 300 ? -8.448  -4.725  11.014  1.00 70.96  ? 297 GLU   A OE1 1 
ATOM   2307 O OE2 . GLU   A 1 300 ? -10.339 -5.549  11.832  1.00 74.85  ? 297 GLU   A OE2 1 
ATOM   2308 N N   . GLN   A 1 301 ? -10.748 -1.759  9.836   1.00 42.92  ? 298 GLN   A N   1 
ATOM   2309 C CA  . GLN   A 1 301 ? -10.076 -1.728  8.541   1.00 45.77  ? 298 GLN   A CA  1 
ATOM   2310 C C   . GLN   A 1 301 ? -9.734  -0.302  8.111   1.00 40.01  ? 298 GLN   A C   1 
ATOM   2311 O O   . GLN   A 1 301 ? -8.673  -0.060  7.517   1.00 38.41  ? 298 GLN   A O   1 
ATOM   2312 C CB  . GLN   A 1 301 ? -10.945 -2.409  7.490   1.00 50.79  ? 298 GLN   A CB  1 
ATOM   2313 C CG  . GLN   A 1 301 ? -10.346 -3.674  6.930   1.00 59.12  ? 298 GLN   A CG  1 
ATOM   2314 C CD  . GLN   A 1 301 ? -11.392 -4.543  6.269   1.00 79.24  ? 298 GLN   A CD  1 
ATOM   2315 O OE1 . GLN   A 1 301 ? -12.592 -4.240  6.315   1.00 88.35  ? 298 GLN   A OE1 1 
ATOM   2316 N NE2 . GLN   A 1 301 ? -10.949 -5.633  5.649   1.00 81.18  ? 298 GLN   A NE2 1 
ATOM   2317 N N   . ASN   A 1 302 ? -10.615 0.658   8.377   1.00 37.33  ? 299 ASN   A N   1 
ATOM   2318 C CA  . ASN   A 1 302 ? -10.290 2.022   7.982   1.00 37.38  ? 299 ASN   A CA  1 
ATOM   2319 C C   . ASN   A 1 302 ? -9.136  2.565   8.812   1.00 35.72  ? 299 ASN   A C   1 
ATOM   2320 O O   . ASN   A 1 302 ? -8.259  3.253   8.271   1.00 34.00  ? 299 ASN   A O   1 
ATOM   2321 C CB  . ASN   A 1 302 ? -11.522 2.922   8.089   1.00 37.43  ? 299 ASN   A CB  1 
ATOM   2322 C CG  . ASN   A 1 302 ? -12.459 2.762   6.905   1.00 36.46  ? 299 ASN   A CG  1 
ATOM   2323 O OD1 . ASN   A 1 302 ? -12.009 2.568   5.770   1.00 35.93  ? 299 ASN   A OD1 1 
ATOM   2324 N ND2 . ASN   A 1 302 ? -13.772 2.827   7.162   1.00 32.79  ? 299 ASN   A ND2 1 
ATOM   2325 N N   . TRP   A 1 303 ? -9.090  2.237   10.115  1.00 30.68  ? 300 TRP   A N   1 
ATOM   2326 C CA  . TRP   A 1 303 ? -7.968  2.703   10.935  1.00 32.78  ? 300 TRP   A CA  1 
ATOM   2327 C C   . TRP   A 1 303 ? -6.639  2.156   10.425  1.00 33.94  ? 300 TRP   A C   1 
ATOM   2328 O O   . TRP   A 1 303 ? -5.639  2.880   10.412  1.00 36.22  ? 300 TRP   A O   1 
ATOM   2329 C CB  . TRP   A 1 303 ? -8.164  2.363   12.420  1.00 27.16  ? 300 TRP   A CB  1 
ATOM   2330 C CG  . TRP   A 1 303 ? -9.246  3.206   13.089  1.00 33.45  ? 300 TRP   A CG  1 
ATOM   2331 C CD1 . TRP   A 1 303 ? -10.421 2.753   13.610  1.00 28.82  ? 300 TRP   A CD1 1 
ATOM   2332 C CD2 . TRP   A 1 303 ? -9.261  4.651   13.270  1.00 31.27  ? 300 TRP   A CD2 1 
ATOM   2333 N NE1 . TRP   A 1 303 ? -11.159 3.805   14.105  1.00 32.07  ? 300 TRP   A NE1 1 
ATOM   2334 C CE2 . TRP   A 1 303 ? -10.473 4.978   13.911  1.00 30.12  ? 300 TRP   A CE2 1 
ATOM   2335 C CE3 . TRP   A 1 303 ? -8.364  5.686   12.962  1.00 29.57  ? 300 TRP   A CE3 1 
ATOM   2336 C CZ2 . TRP   A 1 303 ? -10.823 6.300   14.239  1.00 27.42  ? 300 TRP   A CZ2 1 
ATOM   2337 C CZ3 . TRP   A 1 303 ? -8.719  7.014   13.299  1.00 32.20  ? 300 TRP   A CZ3 1 
ATOM   2338 C CH2 . TRP   A 1 303 ? -9.936  7.297   13.931  1.00 27.66  ? 300 TRP   A CH2 1 
ATOM   2339 N N   . SER   A 1 304 ? -6.608  0.900   9.966   1.00 34.51  ? 301 SER   A N   1 
ATOM   2340 C CA  . SER   A 1 304 ? -5.357  0.356   9.446   1.00 34.24  ? 301 SER   A CA  1 
ATOM   2341 C C   . SER   A 1 304 ? -4.943  1.075   8.174   1.00 35.87  ? 301 SER   A C   1 
ATOM   2342 O O   . SER   A 1 304 ? -3.780  1.453   8.020   1.00 43.51  ? 301 SER   A O   1 
ATOM   2343 C CB  . SER   A 1 304 ? -5.467  -1.150  9.188   1.00 30.17  ? 301 SER   A CB  1 
ATOM   2344 O OG  . SER   A 1 304 ? -6.195  -1.789  10.213  1.00 53.11  ? 301 SER   A OG  1 
ATOM   2345 N N   . ALA   A 1 305 ? -5.882  1.265   7.244   1.00 38.27  ? 302 ALA   A N   1 
ATOM   2346 C CA  . ALA   A 1 305 ? -5.555  1.952   6.000   1.00 36.15  ? 302 ALA   A CA  1 
ATOM   2347 C C   . ALA   A 1 305 ? -5.115  3.390   6.261   1.00 34.12  ? 302 ALA   A C   1 
ATOM   2348 O O   . ALA   A 1 305 ? -4.205  3.898   5.588   1.00 32.46  ? 302 ALA   A O   1 
ATOM   2349 C CB  . ALA   A 1 305 ? -6.754  1.912   5.057   1.00 27.59  ? 302 ALA   A CB  1 
ATOM   2350 N N   . LEU   A 1 306 ? -5.759  4.062   7.231   1.00 29.70  ? 303 LEU   A N   1 
ATOM   2351 C CA  . LEU   A 1 306 ? -5.317  5.393   7.659   1.00 33.30  ? 303 LEU   A CA  1 
ATOM   2352 C C   . LEU   A 1 306 ? -3.843  5.391   8.041   1.00 35.29  ? 303 LEU   A C   1 
ATOM   2353 O O   . LEU   A 1 306 ? -3.067  6.237   7.577   1.00 34.18  ? 303 LEU   A O   1 
ATOM   2354 C CB  . LEU   A 1 306 ? -6.157  5.883   8.842   1.00 33.08  ? 303 LEU   A CB  1 
ATOM   2355 C CG  . LEU   A 1 306 ? -5.901  7.329   9.253   1.00 30.94  ? 303 LEU   A CG  1 
ATOM   2356 C CD1 . LEU   A 1 306 ? -6.307  8.249   8.137   1.00 33.39  ? 303 LEU   A CD1 1 
ATOM   2357 C CD2 . LEU   A 1 306 ? -6.687  7.667   10.475  1.00 34.35  ? 303 LEU   A CD2 1 
ATOM   2358 N N   . HIS   A 1 307 ? -3.436  4.419   8.868   1.00 30.65  ? 304 HIS   A N   1 
ATOM   2359 C CA  . HIS   A 1 307 ? -2.054  4.365   9.324   1.00 34.89  ? 304 HIS   A CA  1 
ATOM   2360 C C   . HIS   A 1 307 ? -1.106  4.037   8.179   1.00 39.41  ? 304 HIS   A C   1 
ATOM   2361 O O   . HIS   A 1 307 ? -0.021  4.617   8.084   1.00 39.45  ? 304 HIS   A O   1 
ATOM   2362 C CB  . HIS   A 1 307 ? -1.913  3.353   10.466  1.00 36.57  ? 304 HIS   A CB  1 
ATOM   2363 C CG  . HIS   A 1 307 ? -2.321  3.889   11.810  1.00 39.19  ? 304 HIS   A CG  1 
ATOM   2364 N ND1 . HIS   A 1 307 ? -1.481  4.652   12.597  1.00 39.65  ? 304 HIS   A ND1 1 
ATOM   2365 C CD2 . HIS   A 1 307 ? -3.480  3.769   12.507  1.00 34.40  ? 304 HIS   A CD2 1 
ATOM   2366 C CE1 . HIS   A 1 307 ? -2.102  4.977   13.719  1.00 35.24  ? 304 HIS   A CE1 1 
ATOM   2367 N NE2 . HIS   A 1 307 ? -3.318  4.457   13.687  1.00 38.30  ? 304 HIS   A NE2 1 
ATOM   2368 N N   . GLU   A 1 308 ? -1.501  3.122   7.292   1.00 39.41  ? 305 GLU   A N   1 
ATOM   2369 C CA  . GLU   A 1 308 ? -0.637  2.756   6.177   1.00 42.73  ? 305 GLU   A CA  1 
ATOM   2370 C C   . GLU   A 1 308 ? -0.514  3.910   5.189   1.00 38.84  ? 305 GLU   A C   1 
ATOM   2371 O O   . GLU   A 1 308 ? 0.582   4.422   4.945   1.00 39.21  ? 305 GLU   A O   1 
ATOM   2372 C CB  . GLU   A 1 308 ? -1.169  1.487   5.499   1.00 49.29  ? 305 GLU   A CB  1 
ATOM   2373 C CG  . GLU   A 1 308 ? -0.293  0.951   4.338   1.00 59.66  ? 305 GLU   A CG  1 
ATOM   2374 C CD  . GLU   A 1 308 ? -0.820  -0.361  3.694   1.00 76.50  ? 305 GLU   A CD  1 
ATOM   2375 O OE1 . GLU   A 1 308 ? -1.902  -0.847  4.127   1.00 78.05  ? 305 GLU   A OE1 1 
ATOM   2376 O OE2 . GLU   A 1 308 ? -0.146  -0.918  2.777   1.00 69.66  ? 305 GLU   A OE2 1 
ATOM   2377 N N   . GLU   A 1 309 ? -1.636  4.369   4.648   1.00 38.11  ? 306 GLU   A N   1 
ATOM   2378 C CA  . GLU   A 1 309 ? -1.589  5.443   3.665   1.00 40.75  ? 306 GLU   A CA  1 
ATOM   2379 C C   . GLU   A 1 309 ? -1.133  6.758   4.299   1.00 42.17  ? 306 GLU   A C   1 
ATOM   2380 O O   . GLU   A 1 309 ? -0.054  7.280   3.980   1.00 43.28  ? 306 GLU   A O   1 
ATOM   2381 C CB  . GLU   A 1 309 ? -2.961  5.576   3.001   1.00 41.46  ? 306 GLU   A CB  1 
ATOM   2382 C CG  . GLU   A 1 309 ? -3.502  4.218   2.524   1.00 45.60  ? 306 GLU   A CG  1 
ATOM   2383 C CD  . GLU   A 1 309 ? -4.808  4.324   1.755   1.00 50.58  ? 306 GLU   A CD  1 
ATOM   2384 O OE1 . GLU   A 1 309 ? -5.181  5.464   1.345   1.00 48.38  ? 306 GLU   A OE1 1 
ATOM   2385 O OE2 . GLU   A 1 309 ? -5.449  3.256   1.570   1.00 44.49  ? 306 GLU   A OE2 1 
ATOM   2386 N N   . LEU   A 1 310 ? -1.926  7.297   5.228   1.00 39.27  ? 307 LEU   A N   1 
ATOM   2387 C CA  . LEU   A 1 310 ? -1.647  8.643   5.712   1.00 37.59  ? 307 LEU   A CA  1 
ATOM   2388 C C   . LEU   A 1 310 ? -0.396  8.673   6.574   1.00 39.34  ? 307 LEU   A C   1 
ATOM   2389 O O   . LEU   A 1 310 ? 0.394   9.619   6.488   1.00 39.41  ? 307 LEU   A O   1 
ATOM   2390 C CB  . LEU   A 1 310 ? -2.844  9.187   6.482   1.00 40.94  ? 307 LEU   A CB  1 
ATOM   2391 C CG  . LEU   A 1 310 ? -2.979  10.705  6.432   1.00 39.75  ? 307 LEU   A CG  1 
ATOM   2392 C CD1 . LEU   A 1 310 ? -3.191  11.150  4.997   1.00 42.12  ? 307 LEU   A CD1 1 
ATOM   2393 C CD2 . LEU   A 1 310 ? -4.138  11.151  7.318   1.00 37.86  ? 307 LEU   A CD2 1 
ATOM   2394 N N   . GLY   A 1 311 ? -0.204  7.650   7.414   1.00 40.58  ? 308 GLY   A N   1 
ATOM   2395 C CA  . GLY   A 1 311 ? 0.973   7.604   8.265   1.00 36.53  ? 308 GLY   A CA  1 
ATOM   2396 C C   . GLY   A 1 311 ? 2.269   7.564   7.478   1.00 38.35  ? 308 GLY   A C   1 
ATOM   2397 O O   . GLY   A 1 311 ? 3.271   8.164   7.882   1.00 34.73  ? 308 GLY   A O   1 
ATOM   2398 N N   . GLY   A 1 312 ? 2.269   6.856   6.342   1.00 38.99  ? 309 GLY   A N   1 
ATOM   2399 C CA  . GLY   A 1 312 ? 3.456   6.837   5.496   1.00 40.33  ? 309 GLY   A CA  1 
ATOM   2400 C C   . GLY   A 1 312 ? 3.810   8.220   4.982   1.00 38.96  ? 309 GLY   A C   1 
ATOM   2401 O O   . GLY   A 1 312 ? 4.942   8.687   5.132   1.00 36.01  ? 309 GLY   A O   1 
ATOM   2402 N N   . LEU   A 1 313 ? 2.823   8.911   4.405   1.00 39.74  ? 310 LEU   A N   1 
ATOM   2403 C CA  . LEU   A 1 313 ? 3.054   10.253  3.887   1.00 42.24  ? 310 LEU   A CA  1 
ATOM   2404 C C   . LEU   A 1 313 ? 3.571   11.201  4.966   1.00 37.43  ? 310 LEU   A C   1 
ATOM   2405 O O   . LEU   A 1 313 ? 4.455   12.021  4.701   1.00 39.91  ? 310 LEU   A O   1 
ATOM   2406 C CB  . LEU   A 1 313 ? 1.765   10.784  3.262   1.00 38.68  ? 310 LEU   A CB  1 
ATOM   2407 C CG  . LEU   A 1 313 ? 1.378   9.956   2.053   1.00 38.29  ? 310 LEU   A CG  1 
ATOM   2408 C CD1 . LEU   A 1 313 ? 0.048   10.397  1.475   1.00 34.18  ? 310 LEU   A CD1 1 
ATOM   2409 C CD2 . LEU   A 1 313 ? 2.489   10.071  1.037   1.00 42.52  ? 310 LEU   A CD2 1 
ATOM   2410 N N   . VAL   A 1 314 ? 3.032   11.111  6.186   1.00 38.18  ? 311 VAL   A N   1 
ATOM   2411 C CA  . VAL   A 1 314 ? 3.497   11.996  7.254   1.00 40.80  ? 311 VAL   A CA  1 
ATOM   2412 C C   . VAL   A 1 314 ? 4.931   11.661  7.612   1.00 45.41  ? 311 VAL   A C   1 
ATOM   2413 O O   . VAL   A 1 314 ? 5.764   12.549  7.852   1.00 45.39  ? 311 VAL   A O   1 
ATOM   2414 C CB  . VAL   A 1 314 ? 2.585   11.887  8.490   1.00 36.98  ? 311 VAL   A CB  1 
ATOM   2415 C CG1 . VAL   A 1 314 ? 3.199   12.637  9.647   1.00 34.03  ? 311 VAL   A CG1 1 
ATOM   2416 C CG2 . VAL   A 1 314 ? 1.177   12.399  8.196   1.00 33.29  ? 311 VAL   A CG2 1 
ATOM   2417 N N   . ARG   A 1 315 ? 5.236   10.365  7.634   1.00 48.39  ? 312 ARG   A N   1 
ATOM   2418 C CA  . ARG   A 1 315 ? 6.537   9.886   8.078   1.00 47.29  ? 312 ARG   A CA  1 
ATOM   2419 C C   . ARG   A 1 315 ? 7.609   10.209  7.050   1.00 49.75  ? 312 ARG   A C   1 
ATOM   2420 O O   . ARG   A 1 315 ? 8.682   10.719  7.393   1.00 54.17  ? 312 ARG   A O   1 
ATOM   2421 C CB  . ARG   A 1 315 ? 6.446   8.382   8.342   1.00 44.28  ? 312 ARG   A CB  1 
ATOM   2422 C CG  . ARG   A 1 315 ? 7.680   7.771   8.904   1.00 53.57  ? 312 ARG   A CG  1 
ATOM   2423 C CD  . ARG   A 1 315 ? 7.366   6.392   9.434   1.00 51.85  ? 312 ARG   A CD  1 
ATOM   2424 N NE  . ARG   A 1 315 ? 6.474   6.451   10.585  1.00 49.86  ? 312 ARG   A NE  1 
ATOM   2425 C CZ  . ARG   A 1 315 ? 5.267   5.901   10.633  1.00 47.46  ? 312 ARG   A CZ  1 
ATOM   2426 N NH1 . ARG   A 1 315 ? 4.731   5.312   9.567   1.00 36.78  ? 312 ARG   A NH1 1 
ATOM   2427 N NH2 . ARG   A 1 315 ? 4.597   5.909   11.790  1.00 42.42  ? 312 ARG   A NH2 1 
ATOM   2428 N N   . ARG   A 1 316 ? 7.323   9.951   5.775   1.00 48.98  ? 313 ARG   A N   1 
ATOM   2429 C CA  . ARG   A 1 316 ? 8.256   10.320  4.721   1.00 50.23  ? 313 ARG   A CA  1 
ATOM   2430 C C   . ARG   A 1 316 ? 8.379   11.829  4.541   1.00 53.15  ? 313 ARG   A C   1 
ATOM   2431 O O   . ARG   A 1 316 ? 9.156   12.262  3.683   1.00 61.12  ? 313 ARG   A O   1 
ATOM   2432 C CB  . ARG   A 1 316 ? 7.832   9.679   3.405   1.00 48.44  ? 313 ARG   A CB  1 
ATOM   2433 C CG  . ARG   A 1 316 ? 8.139   8.207   3.314   1.00 53.52  ? 313 ARG   A CG  1 
ATOM   2434 C CD  . ARG   A 1 316 ? 7.435   7.639   2.113   1.00 53.08  ? 313 ARG   A CD  1 
ATOM   2435 N NE  . ARG   A 1 316 ? 6.274   6.868   2.522   1.00 55.42  ? 313 ARG   A NE  1 
ATOM   2436 C CZ  . ARG   A 1 316 ? 5.169   6.745   1.804   1.00 53.55  ? 313 ARG   A CZ  1 
ATOM   2437 N NH1 . ARG   A 1 316 ? 5.028   7.372   0.640   1.00 53.06  ? 313 ARG   A NH1 1 
ATOM   2438 N NH2 . ARG   A 1 316 ? 4.177   5.983   2.270   1.00 48.63  ? 313 ARG   A NH2 1 
ATOM   2439 N N   . GLN   A 1 317 ? 7.644   12.617  5.329   1.00 50.72  ? 314 GLN   A N   1 
ATOM   2440 C CA  . GLN   A 1 317 ? 7.573   14.077  5.269   1.00 53.44  ? 314 GLN   A CA  1 
ATOM   2441 C C   . GLN   A 1 317 ? 6.898   14.590  4.009   1.00 49.63  ? 314 GLN   A C   1 
ATOM   2442 O O   . GLN   A 1 317 ? 7.026   15.771  3.697   1.00 53.22  ? 314 GLN   A O   1 
ATOM   2443 C CB  . GLN   A 1 317 ? 8.951   14.735  5.393   1.00 54.10  ? 314 GLN   A CB  1 
ATOM   2444 C CG  . GLN   A 1 317 ? 9.644   14.490  6.721   1.00 55.26  ? 314 GLN   A CG  1 
ATOM   2445 C CD  . GLN   A 1 317 ? 10.934  15.291  6.859   1.00 69.81  ? 314 GLN   A CD  1 
ATOM   2446 O OE1 . GLN   A 1 317 ? 11.016  16.228  7.666   1.00 68.82  ? 314 GLN   A OE1 1 
ATOM   2447 N NE2 . GLN   A 1 317 ? 11.950  14.924  6.070   1.00 66.73  ? 314 GLN   A NE2 1 
ATOM   2448 N N   . GLU   A 1 318 ? 6.182   13.742  3.277   1.00 44.75  ? 315 GLU   A N   1 
ATOM   2449 C CA  . GLU   A 1 318 ? 5.456   14.183  2.092   1.00 51.02  ? 315 GLU   A CA  1 
ATOM   2450 C C   . GLU   A 1 318 ? 4.149   14.886  2.442   1.00 50.04  ? 315 GLU   A C   1 
ATOM   2451 O O   . GLU   A 1 318 ? 3.376   15.243  1.545   1.00 48.75  ? 315 GLU   A O   1 
ATOM   2452 C CB  . GLU   A 1 318 ? 5.165   12.992  1.165   1.00 50.66  ? 315 GLU   A CB  1 
ATOM   2453 C CG  . GLU   A 1 318 ? 6.406   12.216  0.688   1.00 60.81  ? 315 GLU   A CG  1 
ATOM   2454 C CD  . GLU   A 1 318 ? 6.071   11.138  -0.354  1.00 69.91  ? 315 GLU   A CD  1 
ATOM   2455 O OE1 . GLU   A 1 318 ? 5.680   11.516  -1.491  1.00 67.89  ? 315 GLU   A OE1 1 
ATOM   2456 O OE2 . GLU   A 1 318 ? 6.187   9.921   -0.032  1.00 64.12  ? 315 GLU   A OE2 1 
ATOM   2457 N N   . LEU   A 1 319 ? 3.878   15.095  3.722   1.00 41.16  ? 316 LEU   A N   1 
ATOM   2458 C CA  . LEU   A 1 319 ? 2.574   15.600  4.101   1.00 40.41  ? 316 LEU   A CA  1 
ATOM   2459 C C   . LEU   A 1 319 ? 2.612   16.018  5.553   1.00 44.39  ? 316 LEU   A C   1 
ATOM   2460 O O   . LEU   A 1 319 ? 2.943   15.207  6.419   1.00 51.48  ? 316 LEU   A O   1 
ATOM   2461 C CB  . LEU   A 1 319 ? 1.519   14.529  3.877   1.00 41.85  ? 316 LEU   A CB  1 
ATOM   2462 C CG  . LEU   A 1 319 ? 0.102   15.051  3.985   1.00 46.78  ? 316 LEU   A CG  1 
ATOM   2463 C CD1 . LEU   A 1 319 ? -0.687  14.572  2.771   1.00 38.67  ? 316 LEU   A CD1 1 
ATOM   2464 C CD2 . LEU   A 1 319 ? -0.490  14.563  5.270   1.00 44.43  ? 316 LEU   A CD2 1 
ATOM   2465 N N   . VAL   A 1 320 ? 2.274   17.265  5.842   1.00 44.34  ? 317 VAL   A N   1 
ATOM   2466 C CA  . VAL   A 1 320 ? 2.638   17.894  7.107   1.00 39.53  ? 317 VAL   A CA  1 
ATOM   2467 C C   . VAL   A 1 320 ? 1.408   17.992  7.998   1.00 43.40  ? 317 VAL   A C   1 
ATOM   2468 O O   . VAL   A 1 320 ? 0.384   18.561  7.599   1.00 41.41  ? 317 VAL   A O   1 
ATOM   2469 C CB  . VAL   A 1 320 ? 3.275   19.273  6.865   1.00 39.67  ? 317 VAL   A CB  1 
ATOM   2470 C CG1 . VAL   A 1 320 ? 3.111   20.141  8.059   1.00 40.18  ? 317 VAL   A CG1 1 
ATOM   2471 C CG2 . VAL   A 1 320 ? 4.749   19.112  6.509   1.00 44.37  ? 317 VAL   A CG2 1 
ATOM   2472 N N   . ALA   A 1 321 ? 1.516   17.452  9.216   1.00 47.35  ? 318 ALA   A N   1 
ATOM   2473 C CA  . ALA   A 1 321 ? 0.418   17.431  10.188  1.00 43.99  ? 318 ALA   A CA  1 
ATOM   2474 C C   . ALA   A 1 321 ? 0.855   18.073  11.509  1.00 45.64  ? 318 ALA   A C   1 
ATOM   2475 O O   . ALA   A 1 321 ? 1.327   17.379  12.415  1.00 51.76  ? 318 ALA   A O   1 
ATOM   2476 C CB  . ALA   A 1 321 ? -0.059  15.997  10.397  1.00 42.48  ? 318 ALA   A CB  1 
ATOM   2477 N N   . HIS   A 1 322 ? 0.609   19.351  11.647  1.00 39.35  ? 319 HIS   A N   1 
ATOM   2478 C CA  . HIS   A 1 322 ? 1.016   20.042  12.847  1.00 48.86  ? 319 HIS   A CA  1 
ATOM   2479 C C   . HIS   A 1 322 ? 0.082   19.926  14.030  1.00 43.41  ? 319 HIS   A C   1 
ATOM   2480 O O   . HIS   A 1 322 ? -1.115  19.869  13.872  1.00 42.66  ? 319 HIS   A O   1 
ATOM   2481 C CB  . HIS   A 1 322 ? 1.212   21.515  12.509  1.00 53.21  ? 319 HIS   A CB  1 
ATOM   2482 C CG  . HIS   A 1 322 ? 2.370   21.775  11.601  1.00 62.00  ? 319 HIS   A CG  1 
ATOM   2483 N ND1 . HIS   A 1 322 ? 2.366   22.780  10.660  1.00 63.19  ? 319 HIS   A ND1 1 
ATOM   2484 C CD2 . HIS   A 1 322 ? 3.571   21.161  11.492  1.00 64.54  ? 319 HIS   A CD2 1 
ATOM   2485 C CE1 . HIS   A 1 322 ? 3.516   22.778  10.013  1.00 60.56  ? 319 HIS   A CE1 1 
ATOM   2486 N NE2 . HIS   A 1 322 ? 4.266   21.806  10.499  1.00 62.96  ? 319 HIS   A NE2 1 
ATOM   2487 N N   . GLU   A 1 323 ? 0.646   19.864  15.222  1.00 48.12  ? 320 GLU   A N   1 
ATOM   2488 C CA  . GLU   A 1 323 ? -0.182  19.877  16.425  1.00 50.22  ? 320 GLU   A CA  1 
ATOM   2489 C C   . GLU   A 1 323 ? 0.380   20.865  17.434  1.00 40.79  ? 320 GLU   A C   1 
ATOM   2490 O O   . GLU   A 1 323 ? 1.595   21.030  17.546  1.00 43.64  ? 320 GLU   A O   1 
ATOM   2491 C CB  . GLU   A 1 323 ? -0.306  18.483  17.080  1.00 45.74  ? 320 GLU   A CB  1 
ATOM   2492 C CG  . GLU   A 1 323 ? 0.986   17.717  17.216  1.00 45.80  ? 320 GLU   A CG  1 
ATOM   2493 C CD  . GLU   A 1 323 ? 0.814   16.390  17.953  1.00 49.31  ? 320 GLU   A CD  1 
ATOM   2494 O OE1 . GLU   A 1 323 ? -0.298  15.816  17.943  1.00 44.99  ? 320 GLU   A OE1 1 
ATOM   2495 O OE2 . GLU   A 1 323 ? 1.799   15.923  18.561  1.00 58.78  ? 320 GLU   A OE2 1 
ATOM   2496 N N   . THR   A 1 324 ? -0.516  21.534  18.148  1.00 42.96  ? 321 THR   A N   1 
ATOM   2497 C CA  . THR   A 1 324 ? -0.174  22.431  19.252  1.00 46.41  ? 321 THR   A CA  1 
ATOM   2498 C C   . THR   A 1 324 ? -0.590  21.732  20.548  1.00 45.58  ? 321 THR   A C   1 
ATOM   2499 O O   . THR   A 1 324 ? -1.777  21.714  20.900  1.00 38.70  ? 321 THR   A O   1 
ATOM   2500 C CB  . THR   A 1 324 ? -0.882  23.782  19.111  1.00 49.21  ? 321 THR   A CB  1 
ATOM   2501 O OG1 . THR   A 1 324 ? -0.676  24.316  17.797  1.00 51.99  ? 321 THR   A OG1 1 
ATOM   2502 C CG2 . THR   A 1 324 ? -0.371  24.779  20.142  1.00 49.64  ? 321 THR   A CG2 1 
ATOM   2503 N N   . VAL   A 1 325 ? 0.383   21.142  21.245  1.00 45.50  ? 322 VAL   A N   1 
ATOM   2504 C CA  . VAL   A 1 325 ? 0.133   20.432  22.501  1.00 41.22  ? 322 VAL   A CA  1 
ATOM   2505 C C   . VAL   A 1 325 ? 0.385   21.405  23.650  1.00 44.47  ? 322 VAL   A C   1 
ATOM   2506 O O   . VAL   A 1 325 ? 1.531   21.648  24.037  1.00 45.67  ? 322 VAL   A O   1 
ATOM   2507 C CB  . VAL   A 1 325 ? 1.003   19.181  22.647  1.00 39.04  ? 322 VAL   A CB  1 
ATOM   2508 C CG1 . VAL   A 1 325 ? 0.606   18.398  23.912  1.00 37.29  ? 322 VAL   A CG1 1 
ATOM   2509 C CG2 . VAL   A 1 325 ? 0.937   18.300  21.399  1.00 38.66  ? 322 VAL   A CG2 1 
ATOM   2510 N N   . GLN   A 1 326 ? -0.699  21.948  24.202  1.00 45.42  ? 323 GLN   A N   1 
ATOM   2511 C CA  . GLN   A 1 326 ? -0.697  22.649  25.480  1.00 42.64  ? 323 GLN   A CA  1 
ATOM   2512 C C   . GLN   A 1 326 ? -0.648  21.659  26.649  1.00 45.75  ? 323 GLN   A C   1 
ATOM   2513 O O   . GLN   A 1 326 ? -1.228  20.571  26.584  1.00 45.69  ? 323 GLN   A O   1 
ATOM   2514 C CB  . GLN   A 1 326 ? -1.957  23.503  25.569  1.00 39.15  ? 323 GLN   A CB  1 
ATOM   2515 C CG  . GLN   A 1 326 ? -2.214  24.105  26.930  1.00 56.49  ? 323 GLN   A CG  1 
ATOM   2516 C CD  . GLN   A 1 326 ? -1.370  25.348  27.200  1.00 63.38  ? 323 GLN   A CD  1 
ATOM   2517 O OE1 . GLN   A 1 326 ? -0.597  25.396  28.179  1.00 50.64  ? 323 GLN   A OE1 1 
ATOM   2518 N NE2 . GLN   A 1 326 ? -1.522  26.369  26.339  1.00 59.22  ? 323 GLN   A NE2 1 
ATOM   2519 N N   . ASP   A 1 327 ? 0.039   22.039  27.733  1.00 45.07  ? 324 ASP   A N   1 
ATOM   2520 C CA  . ASP   A 1 327 ? 0.160   21.173  28.908  1.00 43.08  ? 324 ASP   A CA  1 
ATOM   2521 C C   . ASP   A 1 327 ? -0.651  21.690  30.096  1.00 47.74  ? 324 ASP   A C   1 
ATOM   2522 O O   . ASP   A 1 327 ? -0.716  22.900  30.349  1.00 49.89  ? 324 ASP   A O   1 
ATOM   2523 C CB  . ASP   A 1 327 ? 1.618   20.998  29.335  1.00 39.21  ? 324 ASP   A CB  1 
ATOM   2524 C CG  . ASP   A 1 327 ? 2.413   20.142  28.355  1.00 48.65  ? 324 ASP   A CG  1 
ATOM   2525 O OD1 . ASP   A 1 327 ? 2.099   20.159  27.152  1.00 53.28  ? 324 ASP   A OD1 1 
ATOM   2526 O OD2 . ASP   A 1 327 ? 3.349   19.440  28.777  1.00 45.08  ? 324 ASP   A OD2 1 
ATOM   2527 N N   . GLY   A 1 328 ? -1.273  20.759  30.820  1.00 44.57  ? 325 GLY   A N   1 
ATOM   2528 C CA  . GLY   A 1 328 ? -1.925  21.060  32.079  1.00 32.96  ? 325 GLY   A CA  1 
ATOM   2529 C C   . GLY   A 1 328 ? -3.431  21.005  32.020  1.00 36.67  ? 325 GLY   A C   1 
ATOM   2530 O O   . GLY   A 1 328 ? -4.048  21.820  31.337  1.00 45.96  ? 325 GLY   A O   1 
ATOM   2531 N N   . PHE   A 1 329 ? -4.028  20.055  32.745  1.00 38.95  ? 326 PHE   A N   1 
ATOM   2532 C CA  . PHE   A 1 329 ? -5.483  19.902  32.771  1.00 38.56  ? 326 PHE   A CA  1 
ATOM   2533 C C   . PHE   A 1 329 ? -6.191  21.219  33.035  1.00 43.79  ? 326 PHE   A C   1 
ATOM   2534 O O   . PHE   A 1 329 ? -7.263  21.471  32.471  1.00 40.32  ? 326 PHE   A O   1 
ATOM   2535 C CB  . PHE   A 1 329 ? -5.886  18.881  33.842  1.00 38.48  ? 326 PHE   A CB  1 
ATOM   2536 C CG  . PHE   A 1 329 ? -7.375  18.641  33.935  1.00 38.77  ? 326 PHE   A CG  1 
ATOM   2537 C CD1 . PHE   A 1 329 ? -7.993  17.694  33.127  1.00 37.27  ? 326 PHE   A CD1 1 
ATOM   2538 C CD2 . PHE   A 1 329 ? -8.157  19.343  34.843  1.00 37.72  ? 326 PHE   A CD2 1 
ATOM   2539 C CE1 . PHE   A 1 329 ? -9.369  17.464  33.208  1.00 32.61  ? 326 PHE   A CE1 1 
ATOM   2540 C CE2 . PHE   A 1 329 ? -9.536  19.118  34.927  1.00 37.03  ? 326 PHE   A CE2 1 
ATOM   2541 C CZ  . PHE   A 1 329 ? -10.138 18.171  34.113  1.00 34.52  ? 326 PHE   A CZ  1 
ATOM   2542 N N   . GLU   A 1 330 ? -5.611  22.065  33.895  1.00 45.63  ? 327 GLU   A N   1 
ATOM   2543 C CA  . GLU   A 1 330 ? -6.244  23.323  34.264  1.00 45.96  ? 327 GLU   A CA  1 
ATOM   2544 C C   . GLU   A 1 330 ? -6.352  24.294  33.094  1.00 46.00  ? 327 GLU   A C   1 
ATOM   2545 O O   . GLU   A 1 330 ? -7.176  25.209  33.149  1.00 48.85  ? 327 GLU   A O   1 
ATOM   2546 C CB  . GLU   A 1 330 ? -5.483  23.980  35.433  1.00 47.14  ? 327 GLU   A CB  1 
ATOM   2547 C CG  . GLU   A 1 330 ? -4.065  24.477  35.111  1.00 45.62  ? 327 GLU   A CG  1 
ATOM   2548 C CD  . GLU   A 1 330 ? -3.003  23.369  35.119  1.00 52.67  ? 327 GLU   A CD  1 
ATOM   2549 O OE1 . GLU   A 1 330 ? -3.256  22.241  35.633  1.00 39.88  ? 327 GLU   A OE1 1 
ATOM   2550 O OE2 . GLU   A 1 330 ? -1.893  23.641  34.601  1.00 55.43  ? 327 GLU   A OE2 1 
ATOM   2551 N N   . HIS   A 1 331 ? -5.566  24.117  32.036  1.00 39.64  ? 328 HIS   A N   1 
ATOM   2552 C CA  . HIS   A 1 331 ? -5.600  25.031  30.905  1.00 43.10  ? 328 HIS   A CA  1 
ATOM   2553 C C   . HIS   A 1 331 ? -6.431  24.498  29.735  1.00 45.56  ? 328 HIS   A C   1 
ATOM   2554 O O   . HIS   A 1 331 ? -6.329  25.029  28.622  1.00 42.57  ? 328 HIS   A O   1 
ATOM   2555 C CB  . HIS   A 1 331 ? -4.171  25.351  30.451  1.00 45.51  ? 328 HIS   A CB  1 
ATOM   2556 C CG  . HIS   A 1 331 ? -3.329  25.961  31.519  1.00 51.04  ? 328 HIS   A CG  1 
ATOM   2557 N ND1 . HIS   A 1 331 ? -2.102  25.447  31.881  1.00 57.54  ? 328 HIS   A ND1 1 
ATOM   2558 C CD2 . HIS   A 1 331 ? -3.548  27.022  32.329  1.00 51.92  ? 328 HIS   A CD2 1 
ATOM   2559 C CE1 . HIS   A 1 331 ? -1.598  26.168  32.865  1.00 53.45  ? 328 HIS   A CE1 1 
ATOM   2560 N NE2 . HIS   A 1 331 ? -2.454  27.132  33.155  1.00 51.43  ? 328 HIS   A NE2 1 
ATOM   2561 N N   . ILE   A 1 332 ? -7.250  23.472  29.963  1.00 40.52  ? 329 ILE   A N   1 
ATOM   2562 C CA  . ILE   A 1 332 ? -8.104  22.959  28.890  1.00 43.73  ? 329 ILE   A CA  1 
ATOM   2563 C C   . ILE   A 1 332 ? -9.010  24.059  28.316  1.00 45.93  ? 329 ILE   A C   1 
ATOM   2564 O O   . ILE   A 1 332 ? -8.969  24.280  27.098  1.00 44.15  ? 329 ILE   A O   1 
ATOM   2565 C CB  . ILE   A 1 332 ? -8.880  21.717  29.369  1.00 40.41  ? 329 ILE   A CB  1 
ATOM   2566 C CG1 . ILE   A 1 332 ? -7.958  20.499  29.429  1.00 35.04  ? 329 ILE   A CG1 1 
ATOM   2567 C CG2 . ILE   A 1 332 ? -10.046 21.400  28.461  1.00 37.29  ? 329 ILE   A CG2 1 
ATOM   2568 C CD1 . ILE   A 1 332 ? -8.656  19.280  29.950  1.00 28.71  ? 329 ILE   A CD1 1 
ATOM   2569 N N   . PRO   A 1 333 ? -9.803  24.782  29.121  1.00 48.53  ? 330 PRO   A N   1 
ATOM   2570 C CA  . PRO   A 1 333 ? -10.666 25.817  28.510  1.00 45.37  ? 330 PRO   A CA  1 
ATOM   2571 C C   . PRO   A 1 333 ? -9.893  26.932  27.821  1.00 44.26  ? 330 PRO   A C   1 
ATOM   2572 O O   . PRO   A 1 333 ? -10.322 27.412  26.763  1.00 42.71  ? 330 PRO   A O   1 
ATOM   2573 C CB  . PRO   A 1 333 ? -11.474 26.337  29.708  1.00 41.58  ? 330 PRO   A CB  1 
ATOM   2574 C CG  . PRO   A 1 333 ? -11.474 25.225  30.689  1.00 39.12  ? 330 PRO   A CG  1 
ATOM   2575 C CD  . PRO   A 1 333 ? -10.107 24.612  30.555  1.00 40.23  ? 330 PRO   A CD  1 
ATOM   2576 N N   . ALA   A 1 334 ? -8.767  27.361  28.392  1.00 37.43  ? 331 ALA   A N   1 
ATOM   2577 C CA  . ALA   A 1 334 ? -7.937  28.363  27.730  1.00 40.77  ? 331 ALA   A CA  1 
ATOM   2578 C C   . ALA   A 1 334 ? -7.472  27.874  26.359  1.00 46.79  ? 331 ALA   A C   1 
ATOM   2579 O O   . ALA   A 1 334 ? -7.548  28.610  25.365  1.00 45.16  ? 331 ALA   A O   1 
ATOM   2580 C CB  . ALA   A 1 334 ? -6.737  28.722  28.614  1.00 31.85  ? 331 ALA   A CB  1 
ATOM   2581 N N   . ALA   A 1 335 ? -6.998  26.622  26.284  1.00 42.47  ? 332 ALA   A N   1 
ATOM   2582 C CA  . ALA   A 1 335 ? -6.593  26.057  24.998  1.00 41.14  ? 332 ALA   A CA  1 
ATOM   2583 C C   . ALA   A 1 335 ? -7.771  25.968  24.027  1.00 43.84  ? 332 ALA   A C   1 
ATOM   2584 O O   . ALA   A 1 335 ? -7.622  26.241  22.828  1.00 43.31  ? 332 ALA   A O   1 
ATOM   2585 C CB  . ALA   A 1 335 ? -5.960  24.683  25.203  1.00 31.84  ? 332 ALA   A CB  1 
ATOM   2586 N N   . TYR   A 1 336 ? -8.953  25.595  24.525  1.00 38.75  ? 333 TYR   A N   1 
ATOM   2587 C CA  . TYR   A 1 336 ? -10.140 25.583  23.674  1.00 40.88  ? 333 TYR   A CA  1 
ATOM   2588 C C   . TYR   A 1 336 ? -10.471 26.979  23.170  1.00 43.00  ? 333 TYR   A C   1 
ATOM   2589 O O   . TYR   A 1 336 ? -10.954 27.145  22.041  1.00 39.23  ? 333 TYR   A O   1 
ATOM   2590 C CB  . TYR   A 1 336 ? -11.300 24.995  24.460  1.00 36.33  ? 333 TYR   A CB  1 
ATOM   2591 C CG  . TYR   A 1 336 ? -12.686 25.091  23.877  1.00 38.47  ? 333 TYR   A CG  1 
ATOM   2592 C CD1 . TYR   A 1 336 ? -13.044 24.379  22.727  1.00 36.22  ? 333 TYR   A CD1 1 
ATOM   2593 C CD2 . TYR   A 1 336 ? -13.680 25.819  24.545  1.00 36.91  ? 333 TYR   A CD2 1 
ATOM   2594 C CE1 . TYR   A 1 336 ? -14.351 24.433  22.233  1.00 39.05  ? 333 TYR   A CE1 1 
ATOM   2595 C CE2 . TYR   A 1 336 ? -14.978 25.888  24.064  1.00 36.06  ? 333 TYR   A CE2 1 
ATOM   2596 C CZ  . TYR   A 1 336 ? -15.317 25.196  22.910  1.00 43.84  ? 333 TYR   A CZ  1 
ATOM   2597 O OH  . TYR   A 1 336 ? -16.616 25.263  22.444  1.00 42.86  ? 333 TYR   A OH  1 
ATOM   2598 N N   . GLN   A 1 337 ? -10.207 27.997  23.999  1.00 46.98  ? 334 GLN   A N   1 
ATOM   2599 C CA  . GLN   A 1 337 ? -10.572 29.362  23.646  1.00 45.22  ? 334 GLN   A CA  1 
ATOM   2600 C C   . GLN   A 1 337 ? -9.807  29.830  22.427  1.00 43.30  ? 334 GLN   A C   1 
ATOM   2601 O O   . GLN   A 1 337 ? -10.344 30.599  21.624  1.00 45.42  ? 334 GLN   A O   1 
ATOM   2602 C CB  . GLN   A 1 337 ? -10.309 30.317  24.820  1.00 47.41  ? 334 GLN   A CB  1 
ATOM   2603 C CG  . GLN   A 1 337 ? -10.890 31.733  24.621  1.00 40.22  ? 334 GLN   A CG  1 
ATOM   2604 C CD  . GLN   A 1 337 ? -12.404 31.760  24.790  1.00 47.54  ? 334 GLN   A CD  1 
ATOM   2605 O OE1 . GLN   A 1 337 ? -12.918 31.591  25.895  1.00 55.31  ? 334 GLN   A OE1 1 
ATOM   2606 N NE2 . GLN   A 1 337 ? -13.123 31.946  23.696  1.00 48.79  ? 334 GLN   A NE2 1 
ATOM   2607 N N   . THR   A 1 338 ? -8.557  29.383  22.271  1.00 35.67  ? 335 THR   A N   1 
ATOM   2608 C CA  . THR   A 1 338 ? -7.747  29.871  21.164  1.00 45.11  ? 335 THR   A CA  1 
ATOM   2609 C C   . THR   A 1 338 ? -8.285  29.443  19.803  1.00 48.06  ? 335 THR   A C   1 
ATOM   2610 O O   . THR   A 1 338 ? -7.891  30.028  18.790  1.00 49.79  ? 335 THR   A O   1 
ATOM   2611 C CB  . THR   A 1 338 ? -6.306  29.404  21.308  1.00 44.75  ? 335 THR   A CB  1 
ATOM   2612 O OG1 . THR   A 1 338 ? -6.209  28.007  20.997  1.00 43.41  ? 335 THR   A OG1 1 
ATOM   2613 C CG2 . THR   A 1 338 ? -5.854  29.637  22.697  1.00 37.70  ? 335 THR   A CG2 1 
ATOM   2614 N N   . LEU   A 1 339 ? -9.176  28.451  19.754  1.00 45.82  ? 336 LEU   A N   1 
ATOM   2615 C CA  . LEU   A 1 339 ? -9.800  28.088  18.491  1.00 44.64  ? 336 LEU   A CA  1 
ATOM   2616 C C   . LEU   A 1 339 ? -10.629 29.227  17.922  1.00 47.35  ? 336 LEU   A C   1 
ATOM   2617 O O   . LEU   A 1 339 ? -10.957 29.202  16.731  1.00 46.38  ? 336 LEU   A O   1 
ATOM   2618 C CB  . LEU   A 1 339 ? -10.676 26.846  18.668  1.00 42.47  ? 336 LEU   A CB  1 
ATOM   2619 C CG  . LEU   A 1 339 ? -9.914  25.542  18.909  1.00 43.84  ? 336 LEU   A CG  1 
ATOM   2620 C CD1 . LEU   A 1 339 ? -10.879 24.489  19.327  1.00 37.86  ? 336 LEU   A CD1 1 
ATOM   2621 C CD2 . LEU   A 1 339 ? -9.173  25.112  17.653  1.00 50.87  ? 336 LEU   A CD2 1 
ATOM   2622 N N   . PHE   A 1 340 ? -10.967 30.224  18.741  1.00 45.77  ? 337 PHE   A N   1 
ATOM   2623 C CA  . PHE   A 1 340 ? -11.820 31.328  18.316  1.00 51.54  ? 337 PHE   A CA  1 
ATOM   2624 C C   . PHE   A 1 340 ? -11.147 32.692  18.404  1.00 51.55  ? 337 PHE   A C   1 
ATOM   2625 O O   . PHE   A 1 340 ? -11.794 33.698  18.103  1.00 53.53  ? 337 PHE   A O   1 
ATOM   2626 C CB  . PHE   A 1 340 ? -13.116 31.349  19.136  1.00 43.40  ? 337 PHE   A CB  1 
ATOM   2627 C CG  . PHE   A 1 340 ? -13.773 30.013  19.261  1.00 46.76  ? 337 PHE   A CG  1 
ATOM   2628 C CD1 . PHE   A 1 340 ? -13.441 29.156  20.307  1.00 49.00  ? 337 PHE   A CD1 1 
ATOM   2629 C CD2 . PHE   A 1 340 ? -14.735 29.610  18.348  1.00 42.28  ? 337 PHE   A CD2 1 
ATOM   2630 C CE1 . PHE   A 1 340 ? -14.049 27.914  20.423  1.00 42.73  ? 337 PHE   A CE1 1 
ATOM   2631 C CE2 . PHE   A 1 340 ? -15.354 28.371  18.466  1.00 40.20  ? 337 PHE   A CE2 1 
ATOM   2632 C CZ  . PHE   A 1 340 ? -15.008 27.521  19.499  1.00 36.89  ? 337 PHE   A CZ  1 
ATOM   2633 N N   . SER   A 1 341 ? -9.875  32.757  18.800  1.00 56.24  ? 338 SER   A N   1 
ATOM   2634 C CA  . SER   A 1 341 ? -9.121  34.004  18.854  1.00 59.77  ? 338 SER   A CA  1 
ATOM   2635 C C   . SER   A 1 341 ? -8.689  34.431  17.450  1.00 68.13  ? 338 SER   A C   1 
ATOM   2636 O O   . SER   A 1 341 ? -8.973  33.766  16.446  1.00 68.75  ? 338 SER   A O   1 
ATOM   2637 C CB  . SER   A 1 341 ? -7.891  33.852  19.751  1.00 55.05  ? 338 SER   A CB  1 
ATOM   2638 O OG  . SER   A 1 341 ? -6.881  33.071  19.122  1.00 57.86  ? 338 SER   A OG  1 
ATOM   2639 N N   . ALA   A 1 342 ? -7.983  35.561  17.387  1.00 70.27  ? 339 ALA   A N   1 
ATOM   2640 C CA  . ALA   A 1 342 ? -7.326  36.023  16.173  1.00 71.22  ? 339 ALA   A CA  1 
ATOM   2641 C C   . ALA   A 1 342 ? -5.848  35.655  16.141  1.00 75.35  ? 339 ALA   A C   1 
ATOM   2642 O O   . ALA   A 1 342 ? -5.148  36.014  15.184  1.00 72.71  ? 339 ALA   A O   1 
ATOM   2643 C CB  . ALA   A 1 342 ? -7.492  37.539  16.025  1.00 67.67  ? 339 ALA   A CB  1 
ATOM   2644 N N   . SER   A 1 343 ? -5.366  34.944  17.163  1.00 73.19  ? 340 SER   A N   1 
ATOM   2645 C CA  . SER   A 1 343 ? -3.975  34.510  17.219  1.00 76.45  ? 340 SER   A CA  1 
ATOM   2646 C C   . SER   A 1 343 ? -3.641  33.565  16.063  1.00 74.71  ? 340 SER   A C   1 
ATOM   2647 O O   . SER   A 1 343 ? -4.392  32.628  15.765  1.00 74.15  ? 340 SER   A O   1 
ATOM   2648 C CB  . SER   A 1 343 ? -3.709  33.830  18.566  1.00 74.27  ? 340 SER   A CB  1 
ATOM   2649 O OG  . SER   A 1 343 ? -2.351  33.447  18.707  1.00 76.42  ? 340 SER   A OG  1 
ATOM   2650 N N   . GLU   A 1 344 ? -2.507  33.819  15.408  1.00 72.80  ? 341 GLU   A N   1 
ATOM   2651 C CA  . GLU   A 1 344 ? -2.015  32.973  14.327  1.00 82.13  ? 341 GLU   A CA  1 
ATOM   2652 C C   . GLU   A 1 344 ? -1.186  31.793  14.822  1.00 80.01  ? 341 GLU   A C   1 
ATOM   2653 O O   . GLU   A 1 344 ? -0.721  30.996  13.999  1.00 79.83  ? 341 GLU   A O   1 
ATOM   2654 C CB  . GLU   A 1 344 ? -1.160  33.788  13.341  1.00 81.28  ? 341 GLU   A CB  1 
ATOM   2655 C CG  . GLU   A 1 344 ? -1.692  35.166  12.996  1.00 76.24  ? 341 GLU   A CG  1 
ATOM   2656 C CD  . GLU   A 1 344 ? -0.580  36.114  12.547  1.00 86.98  ? 341 GLU   A CD  1 
ATOM   2657 O OE1 . GLU   A 1 344 ? -0.208  36.077  11.347  1.00 85.23  ? 341 GLU   A OE1 1 
ATOM   2658 O OE2 . GLU   A 1 344 ? -0.064  36.883  13.400  1.00 84.91  ? 341 GLU   A OE2 1 
ATOM   2659 N N   . SER   A 1 345 ? -0.968  31.676  16.134  1.00 76.77  ? 342 SER   A N   1 
ATOM   2660 C CA  . SER   A 1 345 ? -0.129  30.614  16.677  1.00 72.60  ? 342 SER   A CA  1 
ATOM   2661 C C   . SER   A 1 345 ? -0.789  29.240  16.598  1.00 76.16  ? 342 SER   A C   1 
ATOM   2662 O O   . SER   A 1 345 ? -0.120  28.233  16.868  1.00 72.38  ? 342 SER   A O   1 
ATOM   2663 C CB  . SER   A 1 345 ? 0.236   30.941  18.128  1.00 77.07  ? 342 SER   A CB  1 
ATOM   2664 O OG  . SER   A 1 345 ? -0.920  31.265  18.884  1.00 78.29  ? 342 SER   A OG  1 
ATOM   2665 N N   . ASN   A 1 346 ? -2.068  29.174  16.219  1.00 73.42  ? 343 ASN   A N   1 
ATOM   2666 C CA  . ASN   A 1 346 ? -2.810  27.915  16.206  1.00 69.12  ? 343 ASN   A CA  1 
ATOM   2667 C C   . ASN   A 1 346 ? -2.462  27.127  14.950  1.00 67.04  ? 343 ASN   A C   1 
ATOM   2668 O O   . ASN   A 1 346 ? -3.129  27.214  13.917  1.00 68.98  ? 343 ASN   A O   1 
ATOM   2669 C CB  . ASN   A 1 346 ? -4.305  28.172  16.309  1.00 71.00  ? 343 ASN   A CB  1 
ATOM   2670 C CG  . ASN   A 1 346 ? -4.823  27.908  17.701  1.00 62.35  ? 343 ASN   A CG  1 
ATOM   2671 O OD1 . ASN   A 1 346 ? -4.042  27.679  18.633  1.00 53.26  ? 343 ASN   A OD1 1 
ATOM   2672 N ND2 . ASN   A 1 346 ? -6.143  27.941  17.857  1.00 60.01  ? 343 ASN   A ND2 1 
ATOM   2673 N N   . ARG   A 1 347 ? -1.408  26.333  15.053  1.00 60.05  ? 344 ARG   A N   1 
ATOM   2674 C CA  . ARG   A 1 347 ? -0.993  25.438  13.991  1.00 64.71  ? 344 ARG   A CA  1 
ATOM   2675 C C   . ARG   A 1 347 ? -1.621  24.067  14.227  1.00 58.18  ? 344 ARG   A C   1 
ATOM   2676 O O   . ARG   A 1 347 ? -1.340  23.420  15.241  1.00 52.75  ? 344 ARG   A O   1 
ATOM   2677 C CB  . ARG   A 1 347 ? 0.534   25.341  13.938  1.00 63.95  ? 344 ARG   A CB  1 
ATOM   2678 C CG  . ARG   A 1 347 ? 1.230   26.696  13.799  1.00 66.62  ? 344 ARG   A CG  1 
ATOM   2679 C CD  . ARG   A 1 347 ? 1.412   27.080  12.326  1.00 68.91  ? 344 ARG   A CD  1 
ATOM   2680 N NE  . ARG   A 1 347 ? 1.575   28.516  12.111  1.00 72.02  ? 344 ARG   A NE  1 
ATOM   2681 C CZ  . ARG   A 1 347 ? 0.567   29.368  11.973  1.00 71.05  ? 344 ARG   A CZ  1 
ATOM   2682 N NH1 . ARG   A 1 347 ? -0.694  28.964  12.046  1.00 65.85  ? 344 ARG   A NH1 1 
ATOM   2683 N NH2 . ARG   A 1 347 ? 0.829   30.657  11.769  1.00 71.39  ? 344 ARG   A NH2 1 
ATOM   2684 N N   . GLY   A 1 348 ? -2.494  23.645  13.308  1.00 55.48  ? 345 GLY   A N   1 
ATOM   2685 C CA  . GLY   A 1 348 ? -2.944  22.255  13.287  1.00 50.64  ? 345 GLY   A CA  1 
ATOM   2686 C C   . GLY   A 1 348 ? -3.888  21.908  14.427  1.00 44.97  ? 345 GLY   A C   1 
ATOM   2687 O O   . GLY   A 1 348 ? -4.671  22.730  14.898  1.00 44.79  ? 345 GLY   A O   1 
ATOM   2688 N N   . LYS   A 1 349 ? -3.822  20.662  14.864  1.00 41.05  ? 346 LYS   A N   1 
ATOM   2689 C CA  . LYS   A 1 349 ? -4.670  20.191  15.944  1.00 46.31  ? 346 LYS   A CA  1 
ATOM   2690 C C   . LYS   A 1 349 ? -4.187  20.766  17.276  1.00 47.57  ? 346 LYS   A C   1 
ATOM   2691 O O   . LYS   A 1 349 ? -3.012  20.614  17.639  1.00 44.04  ? 346 LYS   A O   1 
ATOM   2692 C CB  . LYS   A 1 349 ? -4.647  18.656  15.973  1.00 43.14  ? 346 LYS   A CB  1 
ATOM   2693 C CG  . LYS   A 1 349 ? -5.617  18.006  16.958  1.00 42.77  ? 346 LYS   A CG  1 
ATOM   2694 C CD  . LYS   A 1 349 ? -7.047  18.024  16.420  1.00 36.50  ? 346 LYS   A CD  1 
ATOM   2695 C CE  . LYS   A 1 349 ? -8.011  18.591  17.441  1.00 39.41  ? 346 LYS   A CE  1 
ATOM   2696 N NZ  . LYS   A 1 349 ? -8.064  20.080  17.332  1.00 48.27  ? 346 LYS   A NZ  1 
ATOM   2697 N N   . VAL   A 1 350 ? -5.084  21.431  18.002  1.00 40.43  ? 347 VAL   A N   1 
ATOM   2698 C CA  . VAL   A 1 350 ? -4.803  21.867  19.364  1.00 43.59  ? 347 VAL   A CA  1 
ATOM   2699 C C   . VAL   A 1 350 ? -5.121  20.721  20.316  1.00 41.35  ? 347 VAL   A C   1 
ATOM   2700 O O   . VAL   A 1 350 ? -6.188  20.108  20.224  1.00 43.95  ? 347 VAL   A O   1 
ATOM   2701 C CB  . VAL   A 1 350 ? -5.615  23.121  19.719  1.00 44.16  ? 347 VAL   A CB  1 
ATOM   2702 C CG1 . VAL   A 1 350 ? -5.233  23.623  21.104  1.00 39.20  ? 347 VAL   A CG1 1 
ATOM   2703 C CG2 . VAL   A 1 350 ? -5.392  24.189  18.666  1.00 42.56  ? 347 VAL   A CG2 1 
ATOM   2704 N N   . LEU   A 1 351 ? -4.190  20.431  21.228  1.00 40.43  ? 348 LEU   A N   1 
ATOM   2705 C CA  . LEU   A 1 351 ? -4.292  19.329  22.181  1.00 41.50  ? 348 LEU   A CA  1 
ATOM   2706 C C   . LEU   A 1 351 ? -3.875  19.787  23.572  1.00 41.74  ? 348 LEU   A C   1 
ATOM   2707 O O   . LEU   A 1 351 ? -3.040  20.684  23.724  1.00 39.69  ? 348 LEU   A O   1 
ATOM   2708 C CB  . LEU   A 1 351 ? -3.375  18.157  21.809  1.00 38.80  ? 348 LEU   A CB  1 
ATOM   2709 C CG  . LEU   A 1 351 ? -3.764  17.317  20.626  1.00 43.35  ? 348 LEU   A CG  1 
ATOM   2710 C CD1 . LEU   A 1 351 ? -2.940  16.033  20.631  1.00 35.85  ? 348 LEU   A CD1 1 
ATOM   2711 C CD2 . LEU   A 1 351 ? -5.271  17.061  20.754  1.00 43.95  ? 348 LEU   A CD2 1 
ATOM   2712 N N   . VAL   A 1 352 ? -4.400  19.122  24.593  1.00 38.53  ? 349 VAL   A N   1 
ATOM   2713 C CA  . VAL   A 1 352 ? -3.910  19.311  25.953  1.00 38.53  ? 349 VAL   A CA  1 
ATOM   2714 C C   . VAL   A 1 352 ? -3.313  17.999  26.446  1.00 37.75  ? 349 VAL   A C   1 
ATOM   2715 O O   . VAL   A 1 352 ? -3.990  16.963  26.456  1.00 39.15  ? 349 VAL   A O   1 
ATOM   2716 C CB  . VAL   A 1 352 ? -5.010  19.807  26.899  1.00 38.60  ? 349 VAL   A CB  1 
ATOM   2717 C CG1 . VAL   A 1 352 ? -4.451  19.946  28.308  1.00 42.79  ? 349 VAL   A CG1 1 
ATOM   2718 C CG2 . VAL   A 1 352 ? -5.547  21.135  26.401  1.00 35.90  ? 349 VAL   A CG2 1 
ATOM   2719 N N   . ARG   A 1 353 ? -2.043  18.037  26.846  1.00 38.30  ? 350 ARG   A N   1 
ATOM   2720 C CA  . ARG   A 1 353 ? -1.447  16.934  27.588  1.00 36.53  ? 350 ARG   A CA  1 
ATOM   2721 C C   . ARG   A 1 353 ? -1.701  17.165  29.070  1.00 40.66  ? 350 ARG   A C   1 
ATOM   2722 O O   . ARG   A 1 353 ? -1.445  18.259  29.579  1.00 42.26  ? 350 ARG   A O   1 
ATOM   2723 C CB  . ARG   A 1 353 ? 0.050   16.819  27.321  1.00 39.43  ? 350 ARG   A CB  1 
ATOM   2724 C CG  . ARG   A 1 353 ? 0.716   15.643  28.005  1.00 37.25  ? 350 ARG   A CG  1 
ATOM   2725 C CD  . ARG   A 1 353 ? 2.138   15.489  27.520  1.00 37.39  ? 350 ARG   A CD  1 
ATOM   2726 N NE  . ARG   A 1 353 ? 2.910   16.715  27.720  1.00 42.18  ? 350 ARG   A NE  1 
ATOM   2727 C CZ  . ARG   A 1 353 ? 4.225   16.815  27.541  1.00 46.33  ? 350 ARG   A CZ  1 
ATOM   2728 N NH1 . ARG   A 1 353 ? 4.965   15.765  27.204  1.00 37.42  ? 350 ARG   A NH1 1 
ATOM   2729 N NH2 . ARG   A 1 353 ? 4.814   18.000  27.690  1.00 41.46  ? 350 ARG   A NH2 1 
ATOM   2730 N N   . VAL   A 1 354 ? -2.222  16.141  29.749  1.00 43.76  ? 351 VAL   A N   1 
ATOM   2731 C CA  . VAL   A 1 354 ? -2.639  16.239  31.157  1.00 48.44  ? 351 VAL   A CA  1 
ATOM   2732 C C   . VAL   A 1 354 ? -1.596  15.715  32.147  1.00 43.63  ? 351 VAL   A C   1 
ATOM   2733 O O   . VAL   A 1 354 ? -0.388  15.780  31.900  1.00 50.65  ? 351 VAL   A O   1 
ATOM   2734 C CB  . VAL   A 1 354 ? -3.965  15.496  31.391  1.00 45.19  ? 351 VAL   A CB  1 
ATOM   2735 C CG1 . VAL   A 1 354 ? -4.209  15.357  32.881  1.00 46.18  ? 351 VAL   A CG1 1 
ATOM   2736 C CG2 . VAL   A 1 354 ? -5.123  16.229  30.718  1.00 37.83  ? 351 VAL   A CG2 1 
ATOM   2737 N N   . LEU   B 1 1   ? -33.389 26.038  -55.981 1.00 49.16  ? -2  LEU   B N   1 
ATOM   2738 C CA  . LEU   B 1 1   ? -33.970 27.350  -55.691 1.00 61.37  ? -2  LEU   B CA  1 
ATOM   2739 C C   . LEU   B 1 1   ? -35.499 27.331  -55.478 1.00 69.50  ? -2  LEU   B C   1 
ATOM   2740 O O   . LEU   B 1 1   ? -36.248 26.566  -56.116 1.00 57.79  ? -2  LEU   B O   1 
ATOM   2741 C CB  . LEU   B 1 1   ? -33.645 28.341  -56.805 1.00 65.20  ? -2  LEU   B CB  1 
ATOM   2742 C CG  . LEU   B 1 1   ? -32.173 28.538  -57.141 1.00 63.87  ? -2  LEU   B CG  1 
ATOM   2743 C CD1 . LEU   B 1 1   ? -32.038 29.434  -58.368 1.00 65.15  ? -2  LEU   B CD1 1 
ATOM   2744 C CD2 . LEU   B 1 1   ? -31.470 29.124  -55.953 1.00 61.74  ? -2  LEU   B CD2 1 
ATOM   2745 N N   . GLY   B 1 2   ? -35.929 28.205  -54.587 1.00 63.05  ? -1  GLY   B N   1 
ATOM   2746 C CA  . GLY   B 1 2   ? -37.313 28.291  -54.173 1.00 55.26  ? -1  GLY   B CA  1 
ATOM   2747 C C   . GLY   B 1 2   ? -37.400 28.811  -52.754 1.00 54.36  ? -1  GLY   B C   1 
ATOM   2748 O O   . GLY   B 1 2   ? -36.427 28.842  -52.008 1.00 52.77  ? -1  GLY   B O   1 
ATOM   2749 N N   . SER   B 1 3   ? -38.600 29.237  -52.390 1.00 46.16  ? 0   SER   B N   1 
ATOM   2750 C CA  . SER   B 1 3   ? -38.868 29.659  -51.033 1.00 46.91  ? 0   SER   B CA  1 
ATOM   2751 C C   . SER   B 1 3   ? -40.185 29.045  -50.584 1.00 42.18  ? 0   SER   B C   1 
ATOM   2752 O O   . SER   B 1 3   ? -40.887 28.385  -51.354 1.00 38.84  ? 0   SER   B O   1 
ATOM   2753 C CB  . SER   B 1 3   ? -38.895 31.187  -50.906 1.00 42.93  ? 0   SER   B CB  1 
ATOM   2754 O OG  . SER   B 1 3   ? -40.103 31.718  -51.403 1.00 43.00  ? 0   SER   B OG  1 
ATOM   2755 N N   . MET   B 1 4   ? -40.532 29.285  -49.323 1.00 41.08  ? 1   MET   B N   1 
ATOM   2756 C CA  . MET   B 1 4   ? -41.675 28.609  -48.724 1.00 39.39  ? 1   MET   B CA  1 
ATOM   2757 C C   . MET   B 1 4   ? -42.173 29.423  -47.542 1.00 34.12  ? 1   MET   B C   1 
ATOM   2758 O O   . MET   B 1 4   ? -41.386 29.743  -46.649 1.00 36.99  ? 1   MET   B O   1 
ATOM   2759 C CB  . MET   B 1 4   ? -41.242 27.223  -48.272 1.00 41.93  ? 1   MET   B CB  1 
ATOM   2760 C CG  . MET   B 1 4   ? -42.330 26.292  -47.878 1.00 47.39  ? 1   MET   B CG  1 
ATOM   2761 S SD  . MET   B 1 4   ? -41.566 24.971  -46.921 1.00 60.45  ? 1   MET   B SD  1 
ATOM   2762 C CE  . MET   B 1 4   ? -42.767 23.666  -47.198 1.00 54.06  ? 1   MET   B CE  1 
ATOM   2763 N N   . LYS   B 1 5   ? -43.462 29.748  -47.525 1.00 31.17  ? 2   LYS   B N   1 
ATOM   2764 C CA  . LYS   B 1 5   ? -44.016 30.466  -46.385 1.00 33.01  ? 2   LYS   B CA  1 
ATOM   2765 C C   . LYS   B 1 5   ? -44.176 29.508  -45.202 1.00 36.35  ? 2   LYS   B C   1 
ATOM   2766 O O   . LYS   B 1 5   ? -44.531 28.331  -45.367 1.00 34.33  ? 2   LYS   B O   1 
ATOM   2767 C CB  . LYS   B 1 5   ? -45.363 31.118  -46.727 1.00 30.97  ? 2   LYS   B CB  1 
ATOM   2768 C CG  . LYS   B 1 5   ? -45.369 32.014  -47.970 1.00 36.81  ? 2   LYS   B CG  1 
ATOM   2769 C CD  . LYS   B 1 5   ? -44.495 33.258  -47.830 1.00 37.26  ? 2   LYS   B CD  1 
ATOM   2770 C CE  . LYS   B 1 5   ? -44.487 34.130  -49.103 1.00 40.78  ? 2   LYS   B CE  1 
ATOM   2771 N NZ  . LYS   B 1 5   ? -43.967 33.433  -50.350 1.00 46.26  ? 2   LYS   B NZ  1 
ATOM   2772 N N   . THR   B 1 6   ? -43.871 30.010  -44.005 1.00 30.30  ? 3   THR   B N   1 
ATOM   2773 C CA  . THR   B 1 6   ? -44.021 29.245  -42.775 1.00 30.94  ? 3   THR   B CA  1 
ATOM   2774 C C   . THR   B 1 6   ? -44.617 30.151  -41.711 1.00 33.43  ? 3   THR   B C   1 
ATOM   2775 O O   . THR   B 1 6   ? -44.716 31.372  -41.874 1.00 30.86  ? 3   THR   B O   1 
ATOM   2776 C CB  . THR   B 1 6   ? -42.677 28.666  -42.271 1.00 32.51  ? 3   THR   B CB  1 
ATOM   2777 O OG1 . THR   B 1 6   ? -41.840 29.719  -41.766 1.00 29.41  ? 3   THR   B OG1 1 
ATOM   2778 C CG2 . THR   B 1 6   ? -41.937 27.966  -43.394 1.00 33.61  ? 3   THR   B CG2 1 
ATOM   2779 N N   . GLU   B 1 7   ? -44.986 29.545  -40.592 1.00 33.42  ? 4   GLU   B N   1 
ATOM   2780 C CA  . GLU   B 1 7   ? -45.373 30.301  -39.420 1.00 30.70  ? 4   GLU   B CA  1 
ATOM   2781 C C   . GLU   B 1 7   ? -44.426 29.974  -38.280 1.00 30.02  ? 4   GLU   B C   1 
ATOM   2782 O O   . GLU   B 1 7   ? -43.950 28.842  -38.152 1.00 31.86  ? 4   GLU   B O   1 
ATOM   2783 C CB  . GLU   B 1 7   ? -46.817 30.018  -39.040 1.00 31.07  ? 4   GLU   B CB  1 
ATOM   2784 C CG  . GLU   B 1 7   ? -47.773 30.851  -39.868 1.00 42.16  ? 4   GLU   B CG  1 
ATOM   2785 C CD  . GLU   B 1 7   ? -49.234 30.451  -39.706 1.00 53.56  ? 4   GLU   B CD  1 
ATOM   2786 O OE1 . GLU   B 1 7   ? -49.519 29.530  -38.892 1.00 49.50  ? 4   GLU   B OE1 1 
ATOM   2787 O OE2 . GLU   B 1 7   ? -50.086 31.059  -40.406 1.00 47.90  ? 4   GLU   B OE2 1 
ATOM   2788 N N   . ARG   B 1 8   ? -44.133 30.989  -37.482 1.00 28.88  ? 5   ARG   B N   1 
ATOM   2789 C CA  . ARG   B 1 8   ? -43.322 30.863  -36.286 1.00 27.35  ? 5   ARG   B CA  1 
ATOM   2790 C C   . ARG   B 1 8   ? -44.015 31.618  -35.162 1.00 29.64  ? 5   ARG   B C   1 
ATOM   2791 O O   . ARG   B 1 8   ? -44.717 32.615  -35.395 1.00 25.47  ? 5   ARG   B O   1 
ATOM   2792 C CB  . ARG   B 1 8   ? -41.901 31.426  -36.490 1.00 25.53  ? 5   ARG   B CB  1 
ATOM   2793 C CG  . ARG   B 1 8   ? -41.175 30.898  -37.709 1.00 30.18  ? 5   ARG   B CG  1 
ATOM   2794 C CD  . ARG   B 1 8   ? -39.782 31.471  -37.803 1.00 28.97  ? 5   ARG   B CD  1 
ATOM   2795 N NE  . ARG   B 1 8   ? -39.846 32.916  -37.942 1.00 32.40  ? 5   ARG   B NE  1 
ATOM   2796 C CZ  . ARG   B 1 8   ? -39.008 33.769  -37.375 1.00 31.05  ? 5   ARG   B CZ  1 
ATOM   2797 N NH1 . ARG   B 1 8   ? -38.007 33.355  -36.606 1.00 27.75  ? 5   ARG   B NH1 1 
ATOM   2798 N NH2 . ARG   B 1 8   ? -39.188 35.070  -37.568 1.00 30.05  ? 5   ARG   B NH2 1 
ATOM   2799 N N   . TRP   B 1 9   ? -43.830 31.123  -33.942 1.00 26.88  ? 6   TRP   B N   1 
ATOM   2800 C CA  . TRP   B 1 9   ? -44.119 31.891  -32.745 1.00 25.67  ? 6   TRP   B CA  1 
ATOM   2801 C C   . TRP   B 1 9   ? -42.817 32.543  -32.296 1.00 28.19  ? 6   TRP   B C   1 
ATOM   2802 O O   . TRP   B 1 9   ? -41.814 31.850  -32.077 1.00 30.34  ? 6   TRP   B O   1 
ATOM   2803 C CB  . TRP   B 1 9   ? -44.696 30.999  -31.651 1.00 27.23  ? 6   TRP   B CB  1 
ATOM   2804 C CG  . TRP   B 1 9   ? -46.140 30.612  -31.866 1.00 32.44  ? 6   TRP   B CG  1 
ATOM   2805 C CD1 . TRP   B 1 9   ? -46.616 29.421  -32.341 1.00 28.79  ? 6   TRP   B CD1 1 
ATOM   2806 C CD2 . TRP   B 1 9   ? -47.290 31.417  -31.576 1.00 29.71  ? 6   TRP   B CD2 1 
ATOM   2807 N NE1 . TRP   B 1 9   ? -47.993 29.443  -32.366 1.00 28.82  ? 6   TRP   B NE1 1 
ATOM   2808 C CE2 . TRP   B 1 9   ? -48.425 30.659  -31.904 1.00 27.03  ? 6   TRP   B CE2 1 
ATOM   2809 C CE3 . TRP   B 1 9   ? -47.464 32.702  -31.052 1.00 29.05  ? 6   TRP   B CE3 1 
ATOM   2810 C CZ2 . TRP   B 1 9   ? -49.711 31.148  -31.742 1.00 31.48  ? 6   TRP   B CZ2 1 
ATOM   2811 C CZ3 . TRP   B 1 9   ? -48.743 33.186  -30.891 1.00 27.43  ? 6   TRP   B CZ3 1 
ATOM   2812 C CH2 . TRP   B 1 9   ? -49.849 32.413  -31.231 1.00 27.57  ? 6   TRP   B CH2 1 
ATOM   2813 N N   . VAL   B 1 10  ? -42.821 33.863  -32.182 1.00 25.52  ? 7   VAL   B N   1 
ATOM   2814 C CA  . VAL   B 1 10  ? -41.633 34.603  -31.792 1.00 27.49  ? 7   VAL   B CA  1 
ATOM   2815 C C   . VAL   B 1 10  ? -41.902 35.222  -30.432 1.00 27.72  ? 7   VAL   B C   1 
ATOM   2816 O O   . VAL   B 1 10  ? -43.056 35.388  -30.019 1.00 25.42  ? 7   VAL   B O   1 
ATOM   2817 C CB  . VAL   B 1 10  ? -41.263 35.688  -32.822 1.00 27.91  ? 7   VAL   B CB  1 
ATOM   2818 C CG1 . VAL   B 1 10  ? -40.932 35.042  -34.157 1.00 27.59  ? 7   VAL   B CG1 1 
ATOM   2819 C CG2 . VAL   B 1 10  ? -42.422 36.689  -32.965 1.00 25.19  ? 7   VAL   B CG2 1 
ATOM   2820 N N   . VAL   B 1 11  ? -40.819 35.559  -29.733 1.00 25.02  ? 8   VAL   B N   1 
ATOM   2821 C CA  . VAL   B 1 11  ? -40.898 36.156  -28.406 1.00 26.63  ? 8   VAL   B CA  1 
ATOM   2822 C C   . VAL   B 1 11  ? -41.082 37.656  -28.610 1.00 28.56  ? 8   VAL   B C   1 
ATOM   2823 O O   . VAL   B 1 11  ? -40.165 38.354  -29.045 1.00 25.05  ? 8   VAL   B O   1 
ATOM   2824 C CB  . VAL   B 1 11  ? -39.649 35.847  -27.560 1.00 30.40  ? 8   VAL   B CB  1 
ATOM   2825 C CG1 . VAL   B 1 11  ? -39.782 36.413  -26.159 1.00 24.62  ? 8   VAL   B CG1 1 
ATOM   2826 C CG2 . VAL   B 1 11  ? -39.391 34.359  -27.482 1.00 26.93  ? 8   VAL   B CG2 1 
ATOM   2827 N N   . ARG   B 1 12  ? -42.285 38.141  -28.308 1.00 35.46  ? 9   ARG   B N   1 
ATOM   2828 C CA  . ARG   B 1 12  ? -42.666 39.539  -28.435 1.00 29.82  ? 9   ARG   B CA  1 
ATOM   2829 C C   . ARG   B 1 12  ? -42.221 40.342  -27.214 1.00 36.60  ? 9   ARG   B C   1 
ATOM   2830 O O   . ARG   B 1 12  ? -41.713 41.472  -27.342 1.00 34.76  ? 9   ARG   B O   1 
ATOM   2831 C CB  . ARG   B 1 12  ? -44.188 39.619  -28.620 1.00 34.94  ? 9   ARG   B CB  1 
ATOM   2832 C CG  . ARG   B 1 12  ? -44.726 40.942  -29.135 1.00 44.65  ? 9   ARG   B CG  1 
ATOM   2833 C CD  . ARG   B 1 12  ? -46.248 41.024  -29.009 1.00 37.76  ? 9   ARG   B CD  1 
ATOM   2834 N NE  . ARG   B 1 12  ? -46.600 41.184  -27.614 1.00 50.18  ? 9   ARG   B NE  1 
ATOM   2835 C CZ  . ARG   B 1 12  ? -46.525 42.334  -26.953 1.00 54.24  ? 9   ARG   B CZ  1 
ATOM   2836 N NH1 . ARG   B 1 12  ? -46.261 43.477  -27.582 1.00 41.34  ? 9   ARG   B NH1 1 
ATOM   2837 N NH2 . ARG   B 1 12  ? -46.702 42.333  -25.625 1.00 44.63  ? 9   ARG   B NH2 1 
ATOM   2838 N N   . GLU   B 1 13  ? -42.394 39.773  -26.021 1.00 36.90  ? 10  GLU   B N   1 
ATOM   2839 C CA  . GLU   B 1 13  ? -42.108 40.495  -24.790 1.00 40.06  ? 10  GLU   B CA  1 
ATOM   2840 C C   . GLU   B 1 13  ? -41.622 39.521  -23.720 1.00 37.33  ? 10  GLU   B C   1 
ATOM   2841 O O   . GLU   B 1 13  ? -42.076 38.372  -23.650 1.00 37.20  ? 10  GLU   B O   1 
ATOM   2842 C CB  . GLU   B 1 13  ? -43.350 41.256  -24.311 1.00 41.44  ? 10  GLU   B CB  1 
ATOM   2843 C CG  . GLU   B 1 13  ? -43.081 42.306  -23.238 1.00 45.24  ? 10  GLU   B CG  1 
ATOM   2844 C CD  . GLU   B 1 13  ? -44.351 43.060  -22.841 1.00 50.17  ? 10  GLU   B CD  1 
ATOM   2845 O OE1 . GLU   B 1 13  ? -45.451 42.611  -23.234 1.00 54.49  ? 10  GLU   B OE1 1 
ATOM   2846 O OE2 . GLU   B 1 13  ? -44.258 44.100  -22.145 1.00 51.98  ? 10  GLU   B OE2 1 
ATOM   2847 N N   . HIS   B 1 14  ? -40.706 39.999  -22.881 1.00 36.64  ? 11  HIS   B N   1 
ATOM   2848 C CA  . HIS   B 1 14  ? -40.220 39.243  -21.726 1.00 37.95  ? 11  HIS   B CA  1 
ATOM   2849 C C   . HIS   B 1 14  ? -41.057 39.561  -20.493 1.00 40.56  ? 11  HIS   B C   1 
ATOM   2850 O O   . HIS   B 1 14  ? -41.142 40.718  -20.072 1.00 42.54  ? 11  HIS   B O   1 
ATOM   2851 C CB  . HIS   B 1 14  ? -38.753 39.552  -21.438 1.00 26.70  ? 11  HIS   B CB  1 
ATOM   2852 C CG  . HIS   B 1 14  ? -37.808 38.949  -22.427 1.00 30.24  ? 11  HIS   B CG  1 
ATOM   2853 N ND1 . HIS   B 1 14  ? -36.608 39.536  -22.765 1.00 24.51  ? 11  HIS   B ND1 1 
ATOM   2854 C CD2 . HIS   B 1 14  ? -37.894 37.814  -23.164 1.00 32.45  ? 11  HIS   B CD2 1 
ATOM   2855 C CE1 . HIS   B 1 14  ? -35.988 38.781  -23.653 1.00 27.66  ? 11  HIS   B CE1 1 
ATOM   2856 N NE2 . HIS   B 1 14  ? -36.748 37.733  -23.917 1.00 28.09  ? 11  HIS   B NE2 1 
ATOM   2857 N N   . VAL   B 1 15  ? -41.649 38.529  -19.902 1.00 40.12  ? 12  VAL   B N   1 
ATOM   2858 C CA  . VAL   B 1 15  ? -42.437 38.651  -18.683 1.00 41.94  ? 12  VAL   B CA  1 
ATOM   2859 C C   . VAL   B 1 15  ? -41.875 37.669  -17.657 1.00 40.46  ? 12  VAL   B C   1 
ATOM   2860 O O   . VAL   B 1 15  ? -41.861 36.456  -17.902 1.00 42.53  ? 12  VAL   B O   1 
ATOM   2861 C CB  . VAL   B 1 15  ? -43.929 38.369  -18.947 1.00 47.50  ? 12  VAL   B CB  1 
ATOM   2862 C CG1 . VAL   B 1 15  ? -44.757 38.400  -17.640 1.00 31.64  ? 12  VAL   B CG1 1 
ATOM   2863 C CG2 . VAL   B 1 15  ? -44.477 39.324  -20.020 1.00 44.23  ? 12  VAL   B CG2 1 
ATOM   2864 N N   . GLU   B 1 16  ? -41.430 38.189  -16.512 1.00 42.02  ? 13  GLU   B N   1 
ATOM   2865 C CA  . GLU   B 1 16  ? -40.993 37.369  -15.382 1.00 45.00  ? 13  GLU   B CA  1 
ATOM   2866 C C   . GLU   B 1 16  ? -42.169 36.634  -14.741 1.00 43.62  ? 13  GLU   B C   1 
ATOM   2867 O O   . GLU   B 1 16  ? -43.344 36.950  -14.972 1.00 42.38  ? 13  GLU   B O   1 
ATOM   2868 C CB  . GLU   B 1 16  ? -40.338 38.227  -14.297 1.00 49.45  ? 13  GLU   B CB  1 
ATOM   2869 C CG  . GLU   B 1 16  ? -39.149 39.050  -14.732 1.00 52.88  ? 13  GLU   B CG  1 
ATOM   2870 C CD  . GLU   B 1 16  ? -37.877 38.247  -14.709 1.00 55.76  ? 13  GLU   B CD  1 
ATOM   2871 O OE1 . GLU   B 1 16  ? -37.955 37.052  -14.355 1.00 63.14  ? 13  GLU   B OE1 1 
ATOM   2872 O OE2 . GLU   B 1 16  ? -36.804 38.798  -15.038 1.00 62.22  ? 13  GLU   B OE2 1 
ATOM   2873 N N   . GLY   B 1 17  ? -41.828 35.671  -13.875 1.00 43.26  ? 14  GLY   B N   1 
ATOM   2874 C CA  . GLY   B 1 17  ? -42.814 34.949  -13.086 1.00 33.18  ? 14  GLY   B CA  1 
ATOM   2875 C C   . GLY   B 1 17  ? -43.612 33.960  -13.918 1.00 41.06  ? 14  GLY   B C   1 
ATOM   2876 O O   . GLY   B 1 17  ? -43.114 33.351  -14.876 1.00 37.80  ? 14  GLY   B O   1 
ATOM   2877 N N   . VAL   B 1 18  ? -44.876 33.796  -13.545 1.00 41.41  ? 15  VAL   B N   1 
ATOM   2878 C CA  . VAL   B 1 18  ? -45.742 32.899  -14.325 1.00 45.22  ? 15  VAL   B CA  1 
ATOM   2879 C C   . VAL   B 1 18  ? -45.966 33.497  -15.711 1.00 45.18  ? 15  VAL   B C   1 
ATOM   2880 O O   . VAL   B 1 18  ? -46.294 34.696  -15.826 1.00 39.93  ? 15  VAL   B O   1 
ATOM   2881 C CB  . VAL   B 1 18  ? -47.072 32.665  -13.606 1.00 40.66  ? 15  VAL   B CB  1 
ATOM   2882 C CG1 . VAL   B 1 18  ? -47.969 31.756  -14.447 1.00 43.12  ? 15  VAL   B CG1 1 
ATOM   2883 C CG2 . VAL   B 1 18  ? -46.829 32.049  -12.250 1.00 39.17  ? 15  VAL   B CG2 1 
ATOM   2884 N N   . PRO   B 1 19  ? -45.792 32.718  -16.778 1.00 45.89  ? 16  PRO   B N   1 
ATOM   2885 C CA  . PRO   B 1 19  ? -45.952 33.270  -18.131 1.00 42.49  ? 16  PRO   B CA  1 
ATOM   2886 C C   . PRO   B 1 19  ? -47.378 33.728  -18.384 1.00 41.79  ? 16  PRO   B C   1 
ATOM   2887 O O   . PRO   B 1 19  ? -48.345 33.086  -17.968 1.00 46.15  ? 16  PRO   B O   1 
ATOM   2888 C CB  . PRO   B 1 19  ? -45.582 32.093  -19.048 1.00 41.46  ? 16  PRO   B CB  1 
ATOM   2889 C CG  . PRO   B 1 19  ? -44.837 31.114  -18.170 1.00 43.26  ? 16  PRO   B CG  1 
ATOM   2890 C CD  . PRO   B 1 19  ? -45.391 31.299  -16.784 1.00 43.17  ? 16  PRO   B CD  1 
ATOM   2891 N N   . ASP   B 1 20  ? -47.499 34.852  -19.072 1.00 44.26  ? 17  ASP   B N   1 
ATOM   2892 C CA  . ASP   B 1 20  ? -48.744 35.253  -19.734 1.00 41.64  ? 17  ASP   B CA  1 
ATOM   2893 C C   . ASP   B 1 20  ? -48.512 34.952  -21.213 1.00 43.47  ? 17  ASP   B C   1 
ATOM   2894 O O   . ASP   B 1 20  ? -47.985 35.780  -21.964 1.00 42.42  ? 17  ASP   B O   1 
ATOM   2895 C CB  . ASP   B 1 20  ? -49.053 36.722  -19.458 1.00 38.54  ? 17  ASP   B CB  1 
ATOM   2896 C CG  . ASP   B 1 20  ? -50.268 37.228  -20.203 1.00 45.18  ? 17  ASP   B CG  1 
ATOM   2897 O OD1 . ASP   B 1 20  ? -50.932 36.446  -20.929 1.00 39.23  ? 17  ASP   B OD1 1 
ATOM   2898 O OD2 . ASP   B 1 20  ? -50.550 38.441  -20.060 1.00 51.59  ? 17  ASP   B OD2 1 
ATOM   2899 N N   . ALA   B 1 21  ? -48.886 33.737  -21.625 1.00 38.40  ? 18  ALA   B N   1 
ATOM   2900 C CA  . ALA   B 1 21  ? -48.425 33.222  -22.907 1.00 36.45  ? 18  ALA   B CA  1 
ATOM   2901 C C   . ALA   B 1 21  ? -48.983 34.010  -24.088 1.00 37.87  ? 18  ALA   B C   1 
ATOM   2902 O O   . ALA   B 1 21  ? -48.328 34.091  -25.136 1.00 36.70  ? 18  ALA   B O   1 
ATOM   2903 C CB  . ALA   B 1 21  ? -48.773 31.738  -23.034 1.00 36.63  ? 18  ALA   B CB  1 
ATOM   2904 N N   . ALA   B 1 22  ? -50.163 34.618  -23.945 1.00 38.22  ? 19  ALA   B N   1 
ATOM   2905 C CA  . ALA   B 1 22  ? -50.697 35.422  -25.037 1.00 38.30  ? 19  ALA   B CA  1 
ATOM   2906 C C   . ALA   B 1 22  ? -50.047 36.800  -25.129 1.00 33.70  ? 19  ALA   B C   1 
ATOM   2907 O O   . ALA   B 1 22  ? -50.091 37.420  -26.191 1.00 42.68  ? 19  ALA   B O   1 
ATOM   2908 C CB  . ALA   B 1 22  ? -52.213 35.567  -24.902 1.00 34.18  ? 19  ALA   B CB  1 
ATOM   2909 N N   . ARG   B 1 23  ? -49.435 37.284  -24.061 1.00 34.19  ? 20  ARG   B N   1 
ATOM   2910 C CA  . ARG   B 1 23  ? -48.722 38.549  -24.131 1.00 36.40  ? 20  ARG   B CA  1 
ATOM   2911 C C   . ARG   B 1 23  ? -47.283 38.367  -24.591 1.00 42.62  ? 20  ARG   B C   1 
ATOM   2912 O O   . ARG   B 1 23  ? -46.716 39.272  -25.221 1.00 45.65  ? 20  ARG   B O   1 
ATOM   2913 C CB  . ARG   B 1 23  ? -48.743 39.227  -22.762 1.00 39.24  ? 20  ARG   B CB  1 
ATOM   2914 C CG  . ARG   B 1 23  ? -47.987 40.547  -22.692 1.00 45.81  ? 20  ARG   B CG  1 
ATOM   2915 C CD  . ARG   B 1 23  ? -47.965 41.032  -21.266 1.00 49.62  ? 20  ARG   B CD  1 
ATOM   2916 N NE  . ARG   B 1 23  ? -47.161 42.227  -21.057 1.00 52.59  ? 20  ARG   B NE  1 
ATOM   2917 C CZ  . ARG   B 1 23  ? -46.846 42.686  -19.851 1.00 55.75  ? 20  ARG   B CZ  1 
ATOM   2918 N NH1 . ARG   B 1 23  ? -47.240 42.061  -18.750 1.00 45.62  ? 20  ARG   B NH1 1 
ATOM   2919 N NH2 . ARG   B 1 23  ? -46.123 43.798  -19.745 1.00 46.93  ? 20  ARG   B NH2 1 
ATOM   2920 N N   . ILE   B 1 24  ? -46.688 37.212  -24.283 1.00 41.55  ? 21  ILE   B N   1 
ATOM   2921 C CA  . ILE   B 1 24  ? -45.275 36.955  -24.540 1.00 39.66  ? 21  ILE   B CA  1 
ATOM   2922 C C   . ILE   B 1 24  ? -45.022 36.648  -26.014 1.00 32.17  ? 21  ILE   B C   1 
ATOM   2923 O O   . ILE   B 1 24  ? -44.011 37.067  -26.581 1.00 30.71  ? 21  ILE   B O   1 
ATOM   2924 C CB  . ILE   B 1 24  ? -44.812 35.806  -23.626 1.00 37.18  ? 21  ILE   B CB  1 
ATOM   2925 C CG1 . ILE   B 1 24  ? -44.741 36.272  -22.172 1.00 37.47  ? 21  ILE   B CG1 1 
ATOM   2926 C CG2 . ILE   B 1 24  ? -43.489 35.209  -24.088 1.00 34.83  ? 21  ILE   B CG2 1 
ATOM   2927 C CD1 . ILE   B 1 24  ? -44.419 35.150  -21.232 1.00 35.15  ? 21  ILE   B CD1 1 
ATOM   2928 N N   . TYR   B 1 25  ? -45.922 35.919  -26.652 1.00 32.35  ? 22  TYR   B N   1 
ATOM   2929 C CA  . TYR   B 1 25  ? -45.680 35.343  -27.961 1.00 27.89  ? 22  TYR   B CA  1 
ATOM   2930 C C   . TYR   B 1 25  ? -46.573 35.994  -29.009 1.00 30.25  ? 22  TYR   B C   1 
ATOM   2931 O O   . TYR   B 1 25  ? -47.617 36.577  -28.709 1.00 30.65  ? 22  TYR   B O   1 
ATOM   2932 C CB  . TYR   B 1 25  ? -45.913 33.827  -27.940 1.00 26.42  ? 22  TYR   B CB  1 
ATOM   2933 C CG  . TYR   B 1 25  ? -45.038 33.105  -26.948 1.00 32.66  ? 22  TYR   B CG  1 
ATOM   2934 C CD1 . TYR   B 1 25  ? -43.718 32.807  -27.251 1.00 31.34  ? 22  TYR   B CD1 1 
ATOM   2935 C CD2 . TYR   B 1 25  ? -45.528 32.733  -25.701 1.00 34.52  ? 22  TYR   B CD2 1 
ATOM   2936 C CE1 . TYR   B 1 25  ? -42.907 32.153  -26.348 1.00 36.02  ? 22  TYR   B CE1 1 
ATOM   2937 C CE2 . TYR   B 1 25  ? -44.721 32.083  -24.780 1.00 37.79  ? 22  TYR   B CE2 1 
ATOM   2938 C CZ  . TYR   B 1 25  ? -43.409 31.796  -25.107 1.00 38.73  ? 22  TYR   B CZ  1 
ATOM   2939 O OH  . TYR   B 1 25  ? -42.603 31.145  -24.197 1.00 33.75  ? 22  TYR   B OH  1 
ATOM   2940 N N   . GLU   B 1 26  ? -46.136 35.862  -30.257 1.00 31.94  ? 23  GLU   B N   1 
ATOM   2941 C CA  . GLU   B 1 26  ? -46.789 36.444  -31.417 1.00 29.35  ? 23  GLU   B CA  1 
ATOM   2942 C C   . GLU   B 1 26  ? -46.543 35.505  -32.574 1.00 30.22  ? 23  GLU   B C   1 
ATOM   2943 O O   . GLU   B 1 26  ? -45.400 35.090  -32.782 1.00 31.76  ? 23  GLU   B O   1 
ATOM   2944 C CB  . GLU   B 1 26  ? -46.216 37.823  -31.733 1.00 28.85  ? 23  GLU   B CB  1 
ATOM   2945 C CG  . GLU   B 1 26  ? -46.595 38.357  -33.079 1.00 31.61  ? 23  GLU   B CG  1 
ATOM   2946 C CD  . GLU   B 1 26  ? -46.512 39.878  -33.144 1.00 38.65  ? 23  GLU   B CD  1 
ATOM   2947 O OE1 . GLU   B 1 26  ? -46.344 40.535  -32.090 1.00 35.25  ? 23  GLU   B OE1 1 
ATOM   2948 O OE2 . GLU   B 1 26  ? -46.613 40.419  -34.261 1.00 41.95  ? 23  GLU   B OE2 1 
ATOM   2949 N N   . LYS   B 1 27  ? -47.601 35.160  -33.304 1.00 26.94  ? 24  LYS   B N   1 
ATOM   2950 C CA  . LYS   B 1 27  ? -47.482 34.286  -34.461 1.00 30.28  ? 24  LYS   B CA  1 
ATOM   2951 C C   . LYS   B 1 27  ? -47.236 35.124  -35.711 1.00 33.35  ? 24  LYS   B C   1 
ATOM   2952 O O   . LYS   B 1 27  ? -47.993 36.061  -35.999 1.00 33.08  ? 24  LYS   B O   1 
ATOM   2953 C CB  . LYS   B 1 27  ? -48.743 33.437  -34.616 1.00 30.54  ? 24  LYS   B CB  1 
ATOM   2954 C CG  . LYS   B 1 27  ? -48.590 32.221  -35.508 1.00 28.18  ? 24  LYS   B CG  1 
ATOM   2955 C CD  . LYS   B 1 27  ? -49.891 31.456  -35.607 1.00 32.75  ? 24  LYS   B CD  1 
ATOM   2956 C CE  . LYS   B 1 27  ? -50.906 32.245  -36.412 1.00 36.61  ? 24  LYS   B CE  1 
ATOM   2957 N NZ  . LYS   B 1 27  ? -52.025 31.384  -36.849 1.00 46.70  ? 24  LYS   B NZ  1 
ATOM   2958 N N   . VAL   B 1 28  ? -46.167 34.796  -36.433 1.00 30.28  ? 25  VAL   B N   1 
ATOM   2959 C CA  . VAL   B 1 28  ? -45.745 35.541  -37.613 1.00 31.63  ? 25  VAL   B CA  1 
ATOM   2960 C C   . VAL   B 1 28  ? -45.568 34.590  -38.792 1.00 31.46  ? 25  VAL   B C   1 
ATOM   2961 O O   . VAL   B 1 28  ? -45.180 33.427  -38.632 1.00 31.02  ? 25  VAL   B O   1 
ATOM   2962 C CB  . VAL   B 1 28  ? -44.432 36.331  -37.362 1.00 29.92  ? 25  VAL   B CB  1 
ATOM   2963 C CG1 . VAL   B 1 28  ? -44.634 37.381  -36.299 1.00 28.63  ? 25  VAL   B CG1 1 
ATOM   2964 C CG2 . VAL   B 1 28  ? -43.336 35.403  -36.965 1.00 27.03  ? 25  VAL   B CG2 1 
ATOM   2965 N N   . GLU   B 1 29  ? -45.857 35.096  -39.992 1.00 37.11  ? 26  GLU   B N   1 
ATOM   2966 C CA  . GLU   B 1 29  ? -45.556 34.379  -41.227 1.00 31.91  ? 26  GLU   B CA  1 
ATOM   2967 C C   . GLU   B 1 29  ? -44.135 34.717  -41.670 1.00 30.93  ? 26  GLU   B C   1 
ATOM   2968 O O   . GLU   B 1 29  ? -43.739 35.885  -41.695 1.00 32.53  ? 26  GLU   B O   1 
ATOM   2969 C CB  . GLU   B 1 29  ? -46.559 34.720  -42.330 1.00 30.64  ? 26  GLU   B CB  1 
ATOM   2970 C CG  . GLU   B 1 29  ? -46.157 34.151  -43.697 1.00 35.54  ? 26  GLU   B CG  1 
ATOM   2971 C CD  . GLU   B 1 29  ? -47.203 34.378  -44.796 1.00 40.70  ? 26  GLU   B CD  1 
ATOM   2972 O OE1 . GLU   B 1 29  ? -48.399 34.102  -44.572 1.00 38.77  ? 26  GLU   B OE1 1 
ATOM   2973 O OE2 . GLU   B 1 29  ? -46.823 34.823  -45.901 1.00 48.96  ? 26  GLU   B OE2 1 
ATOM   2974 N N   . THR   B 1 30  ? -43.364 33.692  -41.997 1.00 31.39  ? 27  THR   B N   1 
ATOM   2975 C CA  . THR   B 1 30  ? -41.971 33.862  -42.361 1.00 29.82  ? 27  THR   B CA  1 
ATOM   2976 C C   . THR   B 1 30  ? -41.714 33.142  -43.672 1.00 34.96  ? 27  THR   B C   1 
ATOM   2977 O O   . THR   B 1 30  ? -42.007 31.948  -43.806 1.00 32.92  ? 27  THR   B O   1 
ATOM   2978 C CB  . THR   B 1 30  ? -41.049 33.323  -41.253 1.00 36.70  ? 27  THR   B CB  1 
ATOM   2979 O OG1 . THR   B 1 30  ? -41.186 34.148  -40.086 1.00 28.53  ? 27  THR   B OG1 1 
ATOM   2980 C CG2 . THR   B 1 30  ? -39.581 33.300  -41.707 1.00 31.18  ? 27  THR   B CG2 1 
ATOM   2981 N N   . GLU   B 1 31  ? -41.191 33.877  -44.643 1.00 38.97  ? 28  GLU   B N   1 
ATOM   2982 C CA  . GLU   B 1 31  ? -40.738 33.262  -45.877 1.00 38.14  ? 28  GLU   B CA  1 
ATOM   2983 C C   . GLU   B 1 31  ? -39.357 32.665  -45.649 1.00 37.82  ? 28  GLU   B C   1 
ATOM   2984 O O   . GLU   B 1 31  ? -38.447 33.344  -45.167 1.00 37.44  ? 28  GLU   B O   1 
ATOM   2985 C CB  . GLU   B 1 31  ? -40.702 34.281  -47.005 1.00 41.00  ? 28  GLU   B CB  1 
ATOM   2986 C CG  . GLU   B 1 31  ? -40.324 33.697  -48.341 1.00 42.60  ? 28  GLU   B CG  1 
ATOM   2987 C CD  . GLU   B 1 31  ? -40.471 34.707  -49.452 1.00 47.95  ? 28  GLU   B CD  1 
ATOM   2988 O OE1 . GLU   B 1 31  ? -41.133 35.744  -49.227 1.00 51.63  ? 28  GLU   B OE1 1 
ATOM   2989 O OE2 . GLU   B 1 31  ? -39.930 34.465  -50.548 1.00 54.02  ? 28  GLU   B OE2 1 
ATOM   2990 N N   . LEU   B 1 32  ? -39.219 31.392  -45.987 1.00 37.34  ? 29  LEU   B N   1 
ATOM   2991 C CA  . LEU   B 1 32  ? -38.013 30.616  -45.770 1.00 34.59  ? 29  LEU   B CA  1 
ATOM   2992 C C   . LEU   B 1 32  ? -37.374 30.360  -47.125 1.00 41.74  ? 29  LEU   B C   1 
ATOM   2993 O O   . LEU   B 1 32  ? -38.028 29.833  -48.035 1.00 43.78  ? 29  LEU   B O   1 
ATOM   2994 C CB  . LEU   B 1 32  ? -38.363 29.305  -45.070 1.00 36.56  ? 29  LEU   B CB  1 
ATOM   2995 C CG  . LEU   B 1 32  ? -37.256 28.437  -44.506 1.00 39.53  ? 29  LEU   B CG  1 
ATOM   2996 C CD1 . LEU   B 1 32  ? -36.497 29.245  -43.518 1.00 37.90  ? 29  LEU   B CD1 1 
ATOM   2997 C CD2 . LEU   B 1 32  ? -37.853 27.213  -43.848 1.00 35.94  ? 29  LEU   B CD2 1 
ATOM   2998 N N   . ASN   B 1 33  ? -36.124 30.783  -47.281 1.00 47.50  ? 30  ASN   B N   1 
ATOM   2999 C CA  . ASN   B 1 33  ? -35.335 30.340  -48.421 1.00 43.04  ? 30  ASN   B CA  1 
ATOM   3000 C C   . ASN   B 1 33  ? -35.114 28.844  -48.262 1.00 44.64  ? 30  ASN   B C   1 
ATOM   3001 O O   . ASN   B 1 33  ? -34.762 28.378  -47.175 1.00 40.12  ? 30  ASN   B O   1 
ATOM   3002 C CB  . ASN   B 1 33  ? -34.002 31.090  -48.472 1.00 44.91  ? 30  ASN   B CB  1 
ATOM   3003 C CG  . ASN   B 1 33  ? -33.498 31.339  -49.894 1.00 50.83  ? 30  ASN   B CG  1 
ATOM   3004 O OD1 . ASN   B 1 33  ? -34.101 30.911  -50.881 1.00 55.02  ? 30  ASN   B OD1 1 
ATOM   3005 N ND2 . ASN   B 1 33  ? -32.386 32.060  -49.996 1.00 48.76  ? 30  ASN   B ND2 1 
ATOM   3006 N N   . THR   B 1 34  ? -35.378 28.079  -49.319 1.00 47.11  ? 31  THR   B N   1 
ATOM   3007 C CA  . THR   B 1 34  ? -35.223 26.635  -49.250 1.00 46.47  ? 31  THR   B CA  1 
ATOM   3008 C C   . THR   B 1 34  ? -34.048 26.142  -50.081 1.00 50.18  ? 31  THR   B C   1 
ATOM   3009 O O   . THR   B 1 34  ? -33.908 24.926  -50.278 1.00 48.67  ? 31  THR   B O   1 
ATOM   3010 C CB  . THR   B 1 34  ? -36.499 25.935  -49.699 1.00 47.49  ? 31  THR   B CB  1 
ATOM   3011 O OG1 . THR   B 1 34  ? -36.833 26.357  -51.023 1.00 50.78  ? 31  THR   B OG1 1 
ATOM   3012 C CG2 . THR   B 1 34  ? -37.637 26.262  -48.732 1.00 45.82  ? 31  THR   B CG2 1 
ATOM   3013 N N   . ARG   B 1 35  ? -33.209 27.057  -50.578 1.00 53.80  ? 32  ARG   B N   1 
ATOM   3014 C CA  . ARG   B 1 35  ? -31.942 26.705  -51.212 1.00 55.83  ? 32  ARG   B CA  1 
ATOM   3015 C C   . ARG   B 1 35  ? -31.001 26.190  -50.125 1.00 51.22  ? 32  ARG   B C   1 
ATOM   3016 O O   . ARG   B 1 35  ? -30.473 26.968  -49.328 1.00 57.55  ? 32  ARG   B O   1 
ATOM   3017 C CB  . ARG   B 1 35  ? -31.364 27.925  -51.940 1.00 55.23  ? 32  ARG   B CB  1 
ATOM   3018 C CG  . ARG   B 1 35  ? -30.297 27.600  -52.960 1.00 59.53  ? 32  ARG   B CG  1 
ATOM   3019 C CD  . ARG   B 1 35  ? -29.170 28.645  -52.950 1.00 70.95  ? 32  ARG   B CD  1 
ATOM   3020 N NE  . ARG   B 1 35  ? -27.888 28.048  -53.314 1.00 77.13  ? 32  ARG   B NE  1 
ATOM   3021 C CZ  . ARG   B 1 35  ? -27.269 28.220  -54.476 1.00 77.60  ? 32  ARG   B CZ  1 
ATOM   3022 N NH1 . ARG   B 1 35  ? -27.733 29.055  -55.390 1.00 73.17  ? 32  ARG   B NH1 1 
ATOM   3023 N NH2 . ARG   B 1 35  ? -26.153 27.539  -54.727 1.00 77.85  ? 32  ARG   B NH2 1 
ATOM   3024 N N   . LEU   B 1 36  ? -30.822 24.875  -50.065 1.00 46.93  ? 33  LEU   B N   1 
ATOM   3025 C CA  . LEU   B 1 36  ? -30.068 24.247  -48.987 1.00 47.16  ? 33  LEU   B CA  1 
ATOM   3026 C C   . LEU   B 1 36  ? -28.563 24.266  -49.242 1.00 55.05  ? 33  LEU   B C   1 
ATOM   3027 O O   . LEU   B 1 36  ? -28.104 24.132  -50.379 1.00 62.42  ? 33  LEU   B O   1 
ATOM   3028 C CB  . LEU   B 1 36  ? -30.517 22.800  -48.806 1.00 45.08  ? 33  LEU   B CB  1 
ATOM   3029 C CG  . LEU   B 1 36  ? -31.971 22.568  -48.429 1.00 49.95  ? 33  LEU   B CG  1 
ATOM   3030 C CD1 . LEU   B 1 36  ? -32.219 21.086  -48.109 1.00 49.64  ? 33  LEU   B CD1 1 
ATOM   3031 C CD2 . LEU   B 1 36  ? -32.329 23.436  -47.254 1.00 45.38  ? 33  LEU   B CD2 1 
ATOM   3032 N N   . GLY   B 1 37  ? -27.795 24.422  -48.171 1.00 54.73  ? 34  GLY   B N   1 
ATOM   3033 C CA  . GLY   B 1 37  ? -26.377 24.159  -48.218 1.00 55.38  ? 34  GLY   B CA  1 
ATOM   3034 C C   . GLY   B 1 37  ? -26.093 22.671  -48.118 1.00 62.02  ? 34  GLY   B C   1 
ATOM   3035 O O   . GLY   B 1 37  ? -26.993 21.848  -47.957 1.00 58.47  ? 34  GLY   B O   1 
ATOM   3036 N N   . GLU   B 1 38  ? -24.802 22.332  -48.197 1.00 67.84  ? 35  GLU   B N   1 
ATOM   3037 C CA  . GLU   B 1 38  ? -24.418 20.938  -48.404 1.00 69.03  ? 35  GLU   B CA  1 
ATOM   3038 C C   . GLU   B 1 38  ? -24.829 20.053  -47.238 1.00 62.90  ? 35  GLU   B C   1 
ATOM   3039 O O   . GLU   B 1 38  ? -25.235 18.903  -47.445 1.00 64.96  ? 35  GLU   B O   1 
ATOM   3040 C CB  . GLU   B 1 38  ? -22.911 20.813  -48.637 1.00 75.45  ? 35  GLU   B CB  1 
ATOM   3041 C CG  . GLU   B 1 38  ? -22.462 21.024  -50.085 1.00 76.15  ? 35  GLU   B CG  1 
ATOM   3042 C CD  . GLU   B 1 38  ? -21.895 22.416  -50.319 1.00 85.97  ? 35  GLU   B CD  1 
ATOM   3043 O OE1 . GLU   B 1 38  ? -22.485 23.398  -49.801 1.00 82.87  ? 35  GLU   B OE1 1 
ATOM   3044 O OE2 . GLU   B 1 38  ? -20.852 22.522  -51.009 1.00 84.08  ? 35  GLU   B OE2 1 
ATOM   3045 N N   . GLU   B 1 39  ? -24.724 20.552  -46.011 1.00 59.09  ? 36  GLU   B N   1 
ATOM   3046 C CA  . GLU   B 1 39  ? -25.075 19.748  -44.849 1.00 60.08  ? 36  GLU   B CA  1 
ATOM   3047 C C   . GLU   B 1 39  ? -26.465 20.065  -44.311 1.00 59.56  ? 36  GLU   B C   1 
ATOM   3048 O O   . GLU   B 1 39  ? -26.907 19.423  -43.348 1.00 57.36  ? 36  GLU   B O   1 
ATOM   3049 C CB  . GLU   B 1 39  ? -24.031 19.924  -43.740 1.00 58.38  ? 36  GLU   B CB  1 
ATOM   3050 C CG  . GLU   B 1 39  ? -22.634 19.456  -44.117 1.00 65.67  ? 36  GLU   B CG  1 
ATOM   3051 C CD  . GLU   B 1 39  ? -21.549 20.473  -43.749 1.00 75.99  ? 36  GLU   B CD  1 
ATOM   3052 O OE1 . GLU   B 1 39  ? -21.272 20.644  -42.537 1.00 68.14  ? 36  GLU   B OE1 1 
ATOM   3053 O OE2 . GLU   B 1 39  ? -20.981 21.110  -44.675 1.00 72.97  ? 36  GLU   B OE2 1 
ATOM   3054 N N   . GLN   B 1 40  ? -27.175 21.007  -44.928 1.00 55.45  ? 37  GLN   B N   1 
ATOM   3055 C CA  . GLN   B 1 40  ? -28.456 21.482  -44.427 1.00 53.79  ? 37  GLN   B CA  1 
ATOM   3056 C C   . GLN   B 1 40  ? -29.623 20.624  -44.898 1.00 51.21  ? 37  GLN   B C   1 
ATOM   3057 O O   . GLN   B 1 40  ? -29.581 19.999  -45.960 1.00 52.80  ? 37  GLN   B O   1 
ATOM   3058 C CB  . GLN   B 1 40  ? -28.696 22.917  -44.868 1.00 50.06  ? 37  GLN   B CB  1 
ATOM   3059 C CG  . GLN   B 1 40  ? -27.708 23.871  -44.309 1.00 47.60  ? 37  GLN   B CG  1 
ATOM   3060 C CD  . GLN   B 1 40  ? -28.108 25.286  -44.583 1.00 51.08  ? 37  GLN   B CD  1 
ATOM   3061 O OE1 . GLN   B 1 40  ? -28.516 25.625  -45.697 1.00 47.83  ? 37  GLN   B OE1 1 
ATOM   3062 N NE2 . GLN   B 1 40  ? -28.035 26.122  -43.559 1.00 51.91  ? 37  GLN   B NE2 1 
ATOM   3063 N N   . MET   B 1 41  ? -30.683 20.627  -44.094 1.00 51.60  ? 38  MET   B N   1 
ATOM   3064 C CA  . MET   B 1 41  ? -31.946 19.983  -44.413 1.00 48.29  ? 38  MET   B CA  1 
ATOM   3065 C C   . MET   B 1 41  ? -33.084 20.996  -44.323 1.00 47.69  ? 38  MET   B C   1 
ATOM   3066 O O   . MET   B 1 41  ? -32.985 22.010  -43.623 1.00 48.83  ? 38  MET   B O   1 
ATOM   3067 C CB  . MET   B 1 41  ? -32.212 18.810  -43.468 1.00 41.60  ? 38  MET   B CB  1 
ATOM   3068 C CG  . MET   B 1 41  ? -31.093 17.771  -43.478 1.00 50.41  ? 38  MET   B CG  1 
ATOM   3069 S SD  . MET   B 1 41  ? -30.681 17.090  -41.848 1.00 54.59  ? 38  MET   B SD  1 
ATOM   3070 C CE  . MET   B 1 41  ? -32.267 16.517  -41.291 1.00 44.67  ? 38  MET   B CE  1 
ATOM   3071 N N   . LEU   B 1 42  ? -34.162 20.726  -45.058 1.00 42.04  ? 39  LEU   B N   1 
ATOM   3072 C CA  . LEU   B 1 42  ? -35.458 21.350  -44.813 1.00 41.61  ? 39  LEU   B CA  1 
ATOM   3073 C C   . LEU   B 1 42  ? -36.331 20.361  -44.041 1.00 42.79  ? 39  LEU   B C   1 
ATOM   3074 O O   . LEU   B 1 42  ? -36.464 19.202  -44.451 1.00 42.95  ? 39  LEU   B O   1 
ATOM   3075 C CB  . LEU   B 1 42  ? -36.132 21.754  -46.124 1.00 40.53  ? 39  LEU   B CB  1 
ATOM   3076 C CG  . LEU   B 1 42  ? -37.564 22.290  -46.087 1.00 44.87  ? 39  LEU   B CG  1 
ATOM   3077 C CD1 . LEU   B 1 42  ? -37.694 23.484  -45.144 1.00 36.94  ? 39  LEU   B CD1 1 
ATOM   3078 C CD2 . LEU   B 1 42  ? -38.016 22.665  -47.492 1.00 42.09  ? 39  LEU   B CD2 1 
ATOM   3079 N N   . LEU   B 1 43  ? -36.917 20.815  -42.926 1.00 35.61  ? 40  LEU   B N   1 
ATOM   3080 C CA  . LEU   B 1 43  ? -37.719 19.963  -42.058 1.00 37.39  ? 40  LEU   B CA  1 
ATOM   3081 C C   . LEU   B 1 43  ? -39.104 20.557  -41.800 1.00 39.59  ? 40  LEU   B C   1 
ATOM   3082 O O   . LEU   B 1 43  ? -39.305 21.776  -41.842 1.00 37.94  ? 40  LEU   B O   1 
ATOM   3083 C CB  . LEU   B 1 43  ? -37.018 19.723  -40.716 1.00 39.18  ? 40  LEU   B CB  1 
ATOM   3084 C CG  . LEU   B 1 43  ? -35.594 19.155  -40.761 1.00 35.87  ? 40  LEU   B CG  1 
ATOM   3085 C CD1 . LEU   B 1 43  ? -34.562 20.242  -40.569 1.00 34.37  ? 40  LEU   B CD1 1 
ATOM   3086 C CD2 . LEU   B 1 43  ? -35.455 18.091  -39.714 1.00 34.87  ? 40  LEU   B CD2 1 
ATOM   3087 N N   . LYS   B 1 44  ? -40.053 19.669  -41.505 1.00 39.76  ? 41  LYS   B N   1 
ATOM   3088 C CA  . LYS   B 1 44  ? -41.444 20.008  -41.227 1.00 36.47  ? 41  LYS   B CA  1 
ATOM   3089 C C   . LYS   B 1 44  ? -41.800 19.470  -39.841 1.00 39.93  ? 41  LYS   B C   1 
ATOM   3090 O O   . LYS   B 1 44  ? -41.550 18.299  -39.536 1.00 41.37  ? 41  LYS   B O   1 
ATOM   3091 C CB  . LYS   B 1 44  ? -42.363 19.440  -42.341 1.00 37.53  ? 41  LYS   B CB  1 
ATOM   3092 C CG  . LYS   B 1 44  ? -43.868 19.354  -42.023 1.00 39.72  ? 41  LYS   B CG  1 
ATOM   3093 C CD  . LYS   B 1 44  ? -44.705 18.933  -43.253 1.00 45.66  ? 41  LYS   B CD  1 
ATOM   3094 C CE  . LYS   B 1 44  ? -45.471 20.130  -43.883 1.00 57.67  ? 41  LYS   B CE  1 
ATOM   3095 N NZ  . LYS   B 1 44  ? -45.763 20.098  -45.383 1.00 51.58  ? 41  LYS   B NZ  1 
ATOM   3096 N N   . THR   B 1 45  ? -42.346 20.330  -38.991 1.00 36.97  ? 42  THR   B N   1 
ATOM   3097 C CA  . THR   B 1 45  ? -42.623 19.954  -37.610 1.00 37.92  ? 42  THR   B CA  1 
ATOM   3098 C C   . THR   B 1 45  ? -43.913 19.150  -37.522 1.00 39.66  ? 42  THR   B C   1 
ATOM   3099 O O   . THR   B 1 45  ? -44.954 19.583  -38.020 1.00 44.50  ? 42  THR   B O   1 
ATOM   3100 C CB  . THR   B 1 45  ? -42.739 21.196  -36.726 1.00 30.52  ? 42  THR   B CB  1 
ATOM   3101 O OG1 . THR   B 1 45  ? -41.647 22.075  -36.998 1.00 34.16  ? 42  THR   B OG1 1 
ATOM   3102 C CG2 . THR   B 1 45  ? -42.695 20.804  -35.277 1.00 30.82  ? 42  THR   B CG2 1 
ATOM   3103 N N   . LEU   B 1 46  ? -43.852 17.994  -36.865 1.00 38.67  ? 43  LEU   B N   1 
ATOM   3104 C CA  . LEU   B 1 46  ? -45.044 17.187  -36.651 1.00 34.82  ? 43  LEU   B CA  1 
ATOM   3105 C C   . LEU   B 1 46  ? -45.620 17.365  -35.260 1.00 37.69  ? 43  LEU   B C   1 
ATOM   3106 O O   . LEU   B 1 46  ? -46.840 17.489  -35.122 1.00 38.98  ? 43  LEU   B O   1 
ATOM   3107 C CB  . LEU   B 1 46  ? -44.739 15.709  -36.904 1.00 38.27  ? 43  LEU   B CB  1 
ATOM   3108 C CG  . LEU   B 1 46  ? -44.097 15.424  -38.272 1.00 40.94  ? 43  LEU   B CG  1 
ATOM   3109 C CD1 . LEU   B 1 46  ? -43.912 13.931  -38.501 1.00 38.46  ? 43  LEU   B CD1 1 
ATOM   3110 C CD2 . LEU   B 1 46  ? -44.889 16.054  -39.417 1.00 39.70  ? 43  LEU   B CD2 1 
ATOM   3111 N N   . TYR   B 1 47  ? -44.764 17.408  -34.230 1.00 41.18  ? 44  TYR   B N   1 
ATOM   3112 C CA  . TYR   B 1 47  ? -45.172 17.660  -32.851 1.00 34.91  ? 44  TYR   B CA  1 
ATOM   3113 C C   . TYR   B 1 47  ? -44.195 18.604  -32.168 1.00 37.02  ? 44  TYR   B C   1 
ATOM   3114 O O   . TYR   B 1 47  ? -43.009 18.647  -32.508 1.00 36.12  ? 44  TYR   B O   1 
ATOM   3115 C CB  . TYR   B 1 47  ? -45.198 16.399  -32.008 1.00 34.77  ? 44  TYR   B CB  1 
ATOM   3116 C CG  . TYR   B 1 47  ? -46.164 15.336  -32.409 1.00 36.96  ? 44  TYR   B CG  1 
ATOM   3117 C CD1 . TYR   B 1 47  ? -45.843 14.405  -33.386 1.00 36.59  ? 44  TYR   B CD1 1 
ATOM   3118 C CD2 . TYR   B 1 47  ? -47.385 15.229  -31.771 1.00 38.73  ? 44  TYR   B CD2 1 
ATOM   3119 C CE1 . TYR   B 1 47  ? -46.739 13.410  -33.729 1.00 42.26  ? 44  TYR   B CE1 1 
ATOM   3120 C CE2 . TYR   B 1 47  ? -48.278 14.244  -32.101 1.00 35.87  ? 44  TYR   B CE2 1 
ATOM   3121 C CZ  . TYR   B 1 47  ? -47.961 13.338  -33.067 1.00 39.44  ? 44  TYR   B CZ  1 
ATOM   3122 O OH  . TYR   B 1 47  ? -48.882 12.367  -33.376 1.00 40.16  ? 44  TYR   B OH  1 
ATOM   3123 N N   . VAL   B 1 48  ? -44.696 19.320  -31.160 1.00 32.19  ? 45  VAL   B N   1 
ATOM   3124 C CA  . VAL   B 1 48  ? -43.866 20.133  -30.283 1.00 31.82  ? 45  VAL   B CA  1 
ATOM   3125 C C   . VAL   B 1 48  ? -44.238 19.833  -28.842 1.00 34.63  ? 45  VAL   B C   1 
ATOM   3126 O O   . VAL   B 1 48  ? -45.400 19.562  -28.512 1.00 33.97  ? 45  VAL   B O   1 
ATOM   3127 C CB  . VAL   B 1 48  ? -43.975 21.664  -30.535 1.00 32.50  ? 45  VAL   B CB  1 
ATOM   3128 C CG1 . VAL   B 1 48  ? -43.478 22.044  -31.944 1.00 38.67  ? 45  VAL   B CG1 1 
ATOM   3129 C CG2 . VAL   B 1 48  ? -45.387 22.169  -30.279 1.00 31.85  ? 45  VAL   B CG2 1 
ATOM   3130 N N   . SER   B 1 49  ? -43.224 19.889  -27.988 1.00 30.70  ? 46  SER   B N   1 
ATOM   3131 C CA  . SER   B 1 49  ? -43.370 19.803  -26.552 1.00 33.37  ? 46  SER   B CA  1 
ATOM   3132 C C   . SER   B 1 49  ? -43.586 21.197  -25.989 1.00 31.66  ? 46  SER   B C   1 
ATOM   3133 O O   . SER   B 1 49  ? -43.069 22.182  -26.521 1.00 33.61  ? 46  SER   B O   1 
ATOM   3134 C CB  . SER   B 1 49  ? -42.116 19.174  -25.929 1.00 37.65  ? 46  SER   B CB  1 
ATOM   3135 O OG  . SER   B 1 49  ? -42.303 18.878  -24.554 1.00 36.39  ? 46  SER   B OG  1 
ATOM   3136 N N   . VAL   B 1 50  ? -44.366 21.279  -24.920 1.00 26.59  ? 47  VAL   B N   1 
ATOM   3137 C CA  . VAL   B 1 50  ? -44.409 22.467  -24.075 1.00 35.89  ? 47  VAL   B CA  1 
ATOM   3138 C C   . VAL   B 1 50  ? -44.003 22.071  -22.652 1.00 34.72  ? 47  VAL   B C   1 
ATOM   3139 O O   . VAL   B 1 50  ? -44.424 21.029  -22.137 1.00 34.51  ? 47  VAL   B O   1 
ATOM   3140 C CB  . VAL   B 1 50  ? -45.795 23.137  -24.110 1.00 36.76  ? 47  VAL   B CB  1 
ATOM   3141 C CG1 . VAL   B 1 50  ? -46.123 23.536  -25.521 1.00 32.92  ? 47  VAL   B CG1 1 
ATOM   3142 C CG2 . VAL   B 1 50  ? -46.871 22.209  -23.574 1.00 34.82  ? 47  VAL   B CG2 1 
ATOM   3143 N N   . ASP   B 1 51  ? -43.149 22.868  -22.034 1.00 35.97  ? 48  ASP   B N   1 
ATOM   3144 C CA  . ASP   B 1 51  ? -42.579 22.430  -20.767 1.00 35.89  ? 48  ASP   B CA  1 
ATOM   3145 C C   . ASP   B 1 51  ? -42.366 23.626  -19.863 1.00 34.58  ? 48  ASP   B C   1 
ATOM   3146 O O   . ASP   B 1 51  ? -42.158 24.743  -20.345 1.00 34.57  ? 48  ASP   B O   1 
ATOM   3147 C CB  . ASP   B 1 51  ? -41.242 21.707  -20.962 1.00 32.52  ? 48  ASP   B CB  1 
ATOM   3148 C CG  . ASP   B 1 51  ? -41.357 20.523  -21.877 1.00 34.81  ? 48  ASP   B CG  1 
ATOM   3149 O OD1 . ASP   B 1 51  ? -41.435 20.731  -23.111 1.00 40.24  ? 48  ASP   B OD1 1 
ATOM   3150 O OD2 . ASP   B 1 51  ? -41.395 19.386  -21.373 1.00 37.29  ? 48  ASP   B OD2 1 
ATOM   3151 N N   . PRO   B 1 52  ? -42.394 23.421  -18.552 1.00 41.06  ? 49  PRO   B N   1 
ATOM   3152 C CA  . PRO   B 1 52  ? -42.103 24.547  -17.652 1.00 39.10  ? 49  PRO   B CA  1 
ATOM   3153 C C   . PRO   B 1 52  ? -40.701 25.098  -17.838 1.00 36.76  ? 49  PRO   B C   1 
ATOM   3154 O O   . PRO   B 1 52  ? -40.499 26.304  -17.642 1.00 37.74  ? 49  PRO   B O   1 
ATOM   3155 C CB  . PRO   B 1 52  ? -42.312 23.949  -16.254 1.00 35.56  ? 49  PRO   B CB  1 
ATOM   3156 C CG  . PRO   B 1 52  ? -43.196 22.743  -16.486 1.00 37.13  ? 49  PRO   B CG  1 
ATOM   3157 C CD  . PRO   B 1 52  ? -42.766 22.196  -17.824 1.00 34.41  ? 49  PRO   B CD  1 
ATOM   3158 N N   . TYR   B 1 53  ? -39.731 24.272  -18.253 1.00 33.37  ? 50  TYR   B N   1 
ATOM   3159 C CA  . TYR   B 1 53  ? -38.389 24.809  -18.456 1.00 32.22  ? 50  TYR   B CA  1 
ATOM   3160 C C   . TYR   B 1 53  ? -38.318 25.791  -19.616 1.00 36.25  ? 50  TYR   B C   1 
ATOM   3161 O O   . TYR   B 1 53  ? -37.323 26.514  -19.732 1.00 38.58  ? 50  TYR   B O   1 
ATOM   3162 C CB  . TYR   B 1 53  ? -37.368 23.685  -18.660 1.00 30.21  ? 50  TYR   B CB  1 
ATOM   3163 C CG  . TYR   B 1 53  ? -37.529 22.814  -19.883 1.00 32.78  ? 50  TYR   B CG  1 
ATOM   3164 C CD1 . TYR   B 1 53  ? -37.249 23.296  -21.163 1.00 33.48  ? 50  TYR   B CD1 1 
ATOM   3165 C CD2 . TYR   B 1 53  ? -37.912 21.491  -19.756 1.00 32.66  ? 50  TYR   B CD2 1 
ATOM   3166 C CE1 . TYR   B 1 53  ? -37.379 22.493  -22.273 1.00 30.12  ? 50  TYR   B CE1 1 
ATOM   3167 C CE2 . TYR   B 1 53  ? -38.026 20.671  -20.857 1.00 30.25  ? 50  TYR   B CE2 1 
ATOM   3168 C CZ  . TYR   B 1 53  ? -37.766 21.173  -22.122 1.00 36.63  ? 50  TYR   B CZ  1 
ATOM   3169 O OH  . TYR   B 1 53  ? -37.901 20.351  -23.245 1.00 36.72  ? 50  TYR   B OH  1 
ATOM   3170 N N   . LEU   B 1 54  ? -39.343 25.839  -20.468 1.00 34.56  ? 51  LEU   B N   1 
ATOM   3171 C CA  . LEU   B 1 54  ? -39.390 26.840  -21.521 1.00 33.78  ? 51  LEU   B CA  1 
ATOM   3172 C C   . LEU   B 1 54  ? -39.517 28.243  -20.960 1.00 34.59  ? 51  LEU   B C   1 
ATOM   3173 O O   . LEU   B 1 54  ? -39.235 29.205  -21.676 1.00 35.47  ? 51  LEU   B O   1 
ATOM   3174 C CB  . LEU   B 1 54  ? -40.551 26.554  -22.476 1.00 32.30  ? 51  LEU   B CB  1 
ATOM   3175 C CG  . LEU   B 1 54  ? -40.377 25.273  -23.293 1.00 34.73  ? 51  LEU   B CG  1 
ATOM   3176 C CD1 . LEU   B 1 54  ? -41.484 25.108  -24.327 1.00 33.86  ? 51  LEU   B CD1 1 
ATOM   3177 C CD2 . LEU   B 1 54  ? -38.988 25.230  -23.953 1.00 28.10  ? 51  LEU   B CD2 1 
ATOM   3178 N N   . GLN   B 1 55  ? -39.913 28.383  -19.694 1.00 34.16  ? 52  GLN   B N   1 
ATOM   3179 C CA  . GLN   B 1 55  ? -40.102 29.716  -19.130 1.00 34.32  ? 52  GLN   B CA  1 
ATOM   3180 C C   . GLN   B 1 55  ? -38.784 30.472  -19.057 1.00 37.22  ? 52  GLN   B C   1 
ATOM   3181 O O   . GLN   B 1 55  ? -38.728 31.672  -19.369 1.00 34.73  ? 52  GLN   B O   1 
ATOM   3182 C CB  . GLN   B 1 55  ? -40.751 29.607  -17.747 1.00 32.82  ? 52  GLN   B CB  1 
ATOM   3183 C CG  . GLN   B 1 55  ? -41.121 30.936  -17.109 1.00 31.77  ? 52  GLN   B CG  1 
ATOM   3184 C CD  . GLN   B 1 55  ? -40.109 31.392  -16.061 1.00 38.80  ? 52  GLN   B CD  1 
ATOM   3185 O OE1 . GLN   B 1 55  ? -39.095 30.731  -15.823 1.00 36.77  ? 52  GLN   B OE1 1 
ATOM   3186 N NE2 . GLN   B 1 55  ? -40.389 32.526  -15.419 1.00 43.07  ? 52  GLN   B NE2 1 
ATOM   3187 N N   . GLY   B 1 56  ? -37.710 29.782  -18.658 1.00 37.73  ? 53  GLY   B N   1 
ATOM   3188 C CA  . GLY   B 1 56  ? -36.392 30.382  -18.560 1.00 32.65  ? 53  GLY   B CA  1 
ATOM   3189 C C   . GLY   B 1 56  ? -35.721 30.517  -19.911 1.00 32.41  ? 53  GLY   B C   1 
ATOM   3190 O O   . GLY   B 1 56  ? -35.103 31.543  -20.197 1.00 34.36  ? 53  GLY   B O   1 
ATOM   3191 N N   . ILE   B 1 57  ? -35.828 29.487  -20.750 1.00 33.43  ? 54  ILE   B N   1 
ATOM   3192 C CA  . ILE   B 1 57  ? -35.365 29.595  -22.128 1.00 31.33  ? 54  ILE   B CA  1 
ATOM   3193 C C   . ILE   B 1 57  ? -35.954 30.833  -22.794 1.00 33.80  ? 54  ILE   B C   1 
ATOM   3194 O O   . ILE   B 1 57  ? -35.248 31.611  -23.445 1.00 33.45  ? 54  ILE   B O   1 
ATOM   3195 C CB  . ILE   B 1 57  ? -35.722 28.321  -22.910 1.00 34.65  ? 54  ILE   B CB  1 
ATOM   3196 C CG1 . ILE   B 1 57  ? -34.847 27.162  -22.444 1.00 39.21  ? 54  ILE   B CG1 1 
ATOM   3197 C CG2 . ILE   B 1 57  ? -35.535 28.554  -24.417 1.00 27.93  ? 54  ILE   B CG2 1 
ATOM   3198 C CD1 . ILE   B 1 57  ? -33.389 27.319  -22.860 1.00 41.33  ? 54  ILE   B CD1 1 
ATOM   3199 N N   . CYS   B 1 58  ? -37.260 31.024  -22.651 1.00 31.13  ? 55  CYS   B N   1 
ATOM   3200 C CA  . CYS   B 1 58  ? -37.902 32.201  -23.215 1.00 30.78  ? 55  CYS   B CA  1 
ATOM   3201 C C   . CYS   B 1 58  ? -37.270 33.480  -22.684 1.00 30.51  ? 55  CYS   B C   1 
ATOM   3202 O O   . CYS   B 1 58  ? -36.950 34.400  -23.446 1.00 34.18  ? 55  CYS   B O   1 
ATOM   3203 C CB  . CYS   B 1 58  ? -39.391 32.165  -22.889 1.00 34.21  ? 55  CYS   B CB  1 
ATOM   3204 S SG  . CYS   B 1 58  ? -40.313 33.584  -23.452 1.00 32.64  ? 55  CYS   B SG  1 
ATOM   3205 N N   . LEU   B 1 59  ? -37.081 33.555  -21.374 1.00 30.43  ? 56  LEU   B N   1 
ATOM   3206 C CA  . LEU   B 1 59  ? -36.495 34.752  -20.788 1.00 36.20  ? 56  LEU   B CA  1 
ATOM   3207 C C   . LEU   B 1 59  ? -35.101 35.028  -21.352 1.00 33.63  ? 56  LEU   B C   1 
ATOM   3208 O O   . LEU   B 1 59  ? -34.664 36.183  -21.387 1.00 31.90  ? 56  LEU   B O   1 
ATOM   3209 C CB  . LEU   B 1 59  ? -36.464 34.625  -19.253 1.00 27.67  ? 56  LEU   B CB  1 
ATOM   3210 C CG  . LEU   B 1 59  ? -37.816 34.848  -18.572 1.00 34.79  ? 56  LEU   B CG  1 
ATOM   3211 C CD1 . LEU   B 1 59  ? -37.795 34.420  -17.084 1.00 33.55  ? 56  LEU   B CD1 1 
ATOM   3212 C CD2 . LEU   B 1 59  ? -38.243 36.299  -18.729 1.00 31.97  ? 56  LEU   B CD2 1 
ATOM   3213 N N   . ASP   B 1 60  ? -34.403 33.996  -21.817 1.00 28.74  ? 57  ASP   B N   1 
ATOM   3214 C CA  . ASP   B 1 60  ? -33.079 34.156  -22.396 1.00 34.23  ? 57  ASP   B CA  1 
ATOM   3215 C C   . ASP   B 1 60  ? -33.098 34.267  -23.915 1.00 36.59  ? 57  ASP   B C   1 
ATOM   3216 O O   . ASP   B 1 60  ? -32.033 34.223  -24.535 1.00 37.81  ? 57  ASP   B O   1 
ATOM   3217 C CB  . ASP   B 1 60  ? -32.183 32.995  -21.968 1.00 35.75  ? 57  ASP   B CB  1 
ATOM   3218 C CG  . ASP   B 1 60  ? -31.781 33.092  -20.502 1.00 38.88  ? 57  ASP   B CG  1 
ATOM   3219 O OD1 . ASP   B 1 60  ? -31.854 34.206  -19.941 1.00 37.93  ? 57  ASP   B OD1 1 
ATOM   3220 O OD2 . ASP   B 1 60  ? -31.392 32.067  -19.914 1.00 40.25  ? 57  ASP   B OD2 1 
ATOM   3221 N N   . THR   B 1 61  ? -34.282 34.402  -24.526 1.00 30.82  ? 58  THR   B N   1 
ATOM   3222 C CA  . THR   B 1 61  ? -34.415 34.430  -25.970 1.00 30.33  ? 58  THR   B CA  1 
ATOM   3223 C C   . THR   B 1 61  ? -34.522 35.876  -26.418 1.00 32.56  ? 58  THR   B C   1 
ATOM   3224 O O   . THR   B 1 61  ? -35.449 36.569  -25.976 1.00 32.72  ? 58  THR   B O   1 
ATOM   3225 C CB  . THR   B 1 61  ? -35.658 33.656  -26.392 1.00 30.81  ? 58  THR   B CB  1 
ATOM   3226 O OG1 . THR   B 1 61  ? -35.558 32.310  -25.927 1.00 30.91  ? 58  THR   B OG1 1 
ATOM   3227 C CG2 . THR   B 1 61  ? -35.833 33.659  -27.908 1.00 27.69  ? 58  THR   B CG2 1 
ATOM   3228 N N   . PRO   B 1 62  ? -33.620 36.394  -27.247 1.00 32.20  ? 59  PRO   B N   1 
ATOM   3229 C CA  . PRO   B 1 62  ? -33.741 37.806  -27.640 1.00 28.96  ? 59  PRO   B CA  1 
ATOM   3230 C C   . PRO   B 1 62  ? -35.063 38.061  -28.348 1.00 27.85  ? 59  PRO   B C   1 
ATOM   3231 O O   . PRO   B 1 62  ? -35.595 37.197  -29.042 1.00 28.60  ? 59  PRO   B O   1 
ATOM   3232 C CB  . PRO   B 1 62  ? -32.540 38.038  -28.567 1.00 28.91  ? 59  PRO   B CB  1 
ATOM   3233 C CG  . PRO   B 1 62  ? -31.834 36.727  -28.710 1.00 29.76  ? 59  PRO   B CG  1 
ATOM   3234 C CD  . PRO   B 1 62  ? -32.346 35.781  -27.664 1.00 30.42  ? 59  PRO   B CD  1 
ATOM   3235 N N   . ILE   B 1 63  ? -35.596 39.267  -28.134 1.00 27.71  ? 60  ILE   B N   1 
ATOM   3236 C CA  . ILE   B 1 63  ? -36.874 39.669  -28.711 1.00 27.26  ? 60  ILE   B CA  1 
ATOM   3237 C C   . ILE   B 1 63  ? -36.858 39.512  -30.223 1.00 27.96  ? 60  ILE   B C   1 
ATOM   3238 O O   . ILE   B 1 63  ? -35.920 39.942  -30.907 1.00 29.97  ? 60  ILE   B O   1 
ATOM   3239 C CB  . ILE   B 1 63  ? -37.182 41.128  -28.324 1.00 32.24  ? 60  ILE   B CB  1 
ATOM   3240 C CG1 . ILE   B 1 63  ? -37.268 41.279  -26.807 1.00 28.48  ? 60  ILE   B CG1 1 
ATOM   3241 C CG2 . ILE   B 1 63  ? -38.447 41.620  -28.996 1.00 24.55  ? 60  ILE   B CG2 1 
ATOM   3242 C CD1 . ILE   B 1 63  ? -38.252 40.347  -26.191 1.00 30.45  ? 60  ILE   B CD1 1 
ATOM   3243 N N   . GLY   B 1 64  ? -37.931 38.934  -30.760 1.00 29.27  ? 61  GLY   B N   1 
ATOM   3244 C CA  . GLY   B 1 64  ? -38.029 38.619  -32.159 1.00 23.41  ? 61  GLY   B CA  1 
ATOM   3245 C C   . GLY   B 1 64  ? -37.555 37.229  -32.536 1.00 27.53  ? 61  GLY   B C   1 
ATOM   3246 O O   . GLY   B 1 64  ? -37.887 36.749  -33.622 1.00 29.23  ? 61  GLY   B O   1 
ATOM   3247 N N   . ASP   B 1 65  ? -36.771 36.566  -31.695 1.00 27.43  ? 62  ASP   B N   1 
ATOM   3248 C CA  . ASP   B 1 65  ? -36.380 35.225  -32.095 1.00 30.12  ? 62  ASP   B CA  1 
ATOM   3249 C C   . ASP   B 1 65  ? -37.519 34.237  -31.857 1.00 30.06  ? 62  ASP   B C   1 
ATOM   3250 O O   . ASP   B 1 65  ? -38.459 34.498  -31.098 1.00 28.65  ? 62  ASP   B O   1 
ATOM   3251 C CB  . ASP   B 1 65  ? -35.128 34.774  -31.354 1.00 28.30  ? 62  ASP   B CB  1 
ATOM   3252 C CG  . ASP   B 1 65  ? -33.870 35.383  -31.933 1.00 34.50  ? 62  ASP   B CG  1 
ATOM   3253 O OD1 . ASP   B 1 65  ? -33.985 36.237  -32.839 1.00 30.46  ? 62  ASP   B OD1 1 
ATOM   3254 O OD2 . ASP   B 1 65  ? -32.763 35.010  -31.485 1.00 39.98  ? 62  ASP   B OD2 1 
ATOM   3255 N N   . HIS   B 1 66  ? -37.435 33.096  -32.535 1.00 26.11  ? 63  HIS   B N   1 
ATOM   3256 C CA  . HIS   B 1 66  ? -38.455 32.079  -32.366 1.00 28.40  ? 63  HIS   B CA  1 
ATOM   3257 C C   . HIS   B 1 66  ? -38.267 31.353  -31.032 1.00 32.99  ? 63  HIS   B C   1 
ATOM   3258 O O   . HIS   B 1 66  ? -37.167 31.300  -30.461 1.00 32.67  ? 63  HIS   B O   1 
ATOM   3259 C CB  . HIS   B 1 66  ? -38.430 31.096  -33.534 1.00 29.38  ? 63  HIS   B CB  1 
ATOM   3260 C CG  . HIS   B 1 66  ? -37.355 30.059  -33.431 1.00 32.12  ? 63  HIS   B CG  1 
ATOM   3261 N ND1 . HIS   B 1 66  ? -36.091 30.243  -33.947 1.00 28.93  ? 63  HIS   B ND1 1 
ATOM   3262 C CD2 . HIS   B 1 66  ? -37.360 28.822  -32.875 1.00 29.31  ? 63  HIS   B CD2 1 
ATOM   3263 C CE1 . HIS   B 1 66  ? -35.360 29.170  -33.705 1.00 28.93  ? 63  HIS   B CE1 1 
ATOM   3264 N NE2 . HIS   B 1 66  ? -36.107 28.292  -33.060 1.00 32.23  ? 63  HIS   B NE2 1 
ATOM   3265 N N   . MET   B 1 67  ? -39.366 30.822  -30.513 1.00 29.67  ? 64  MET   B N   1 
ATOM   3266 C CA  . MET   B 1 67  ? -39.325 30.120  -29.240 1.00 33.04  ? 64  MET   B CA  1 
ATOM   3267 C C   . MET   B 1 67  ? -38.805 28.707  -29.473 1.00 31.98  ? 64  MET   B C   1 
ATOM   3268 O O   . MET   B 1 67  ? -39.380 27.957  -30.273 1.00 30.05  ? 64  MET   B O   1 
ATOM   3269 C CB  . MET   B 1 67  ? -40.710 30.098  -28.592 1.00 28.94  ? 64  MET   B CB  1 
ATOM   3270 C CG  . MET   B 1 67  ? -40.738 29.446  -27.221 1.00 29.13  ? 64  MET   B CG  1 
ATOM   3271 S SD  . MET   B 1 67  ? -39.838 30.280  -25.902 1.00 28.48  ? 64  MET   B SD  1 
ATOM   3272 C CE  . MET   B 1 67  ? -39.061 28.866  -25.134 1.00 35.99  ? 64  MET   B CE  1 
ATOM   3273 N N   . GLY   B 1 68  ? -37.712 28.353  -28.792 1.00 29.04  ? 65  GLY   B N   1 
ATOM   3274 C CA  . GLY   B 1 68  ? -37.211 26.995  -28.865 1.00 27.98  ? 65  GLY   B CA  1 
ATOM   3275 C C   . GLY   B 1 68  ? -38.088 26.024  -28.094 1.00 31.10  ? 65  GLY   B C   1 
ATOM   3276 O O   . GLY   B 1 68  ? -38.770 26.389  -27.137 1.00 29.57  ? 65  GLY   B O   1 
ATOM   3277 N N   . ALA   B 1 69  ? -38.078 24.766  -28.537 1.00 29.07  ? 66  ALA   B N   1 
ATOM   3278 C CA  . ALA   B 1 69  ? -38.797 23.679  -27.879 1.00 30.86  ? 66  ALA   B CA  1 
ATOM   3279 C C   . ALA   B 1 69  ? -38.357 22.362  -28.499 1.00 31.91  ? 66  ALA   B C   1 
ATOM   3280 O O   . ALA   B 1 69  ? -37.803 22.328  -29.600 1.00 28.05  ? 66  ALA   B O   1 
ATOM   3281 C CB  . ALA   B 1 69  ? -40.315 23.833  -28.002 1.00 30.67  ? 66  ALA   B CB  1 
ATOM   3282 N N   . ASP   B 1 70  ? -38.619 21.276  -27.780 1.00 34.30  ? 67  ASP   B N   1 
ATOM   3283 C CA  . ASP   B 1 70  ? -38.365 19.946  -28.315 1.00 33.43  ? 67  ASP   B CA  1 
ATOM   3284 C C   . ASP   B 1 70  ? -39.442 19.588  -29.341 1.00 35.04  ? 67  ASP   B C   1 
ATOM   3285 O O   . ASP   B 1 70  ? -40.634 19.841  -29.129 1.00 32.49  ? 67  ASP   B O   1 
ATOM   3286 C CB  . ASP   B 1 70  ? -38.325 18.915  -27.177 1.00 35.63  ? 67  ASP   B CB  1 
ATOM   3287 C CG  . ASP   B 1 70  ? -37.662 17.587  -27.597 1.00 44.83  ? 67  ASP   B CG  1 
ATOM   3288 O OD1 . ASP   B 1 70  ? -37.116 17.515  -28.729 1.00 44.43  ? 67  ASP   B OD1 1 
ATOM   3289 O OD2 . ASP   B 1 70  ? -37.700 16.607  -26.807 1.00 48.44  ? 67  ASP   B OD2 1 
ATOM   3290 N N   . SER   B 1 71  ? -39.025 18.992  -30.458 1.00 33.08  ? 68  SER   B N   1 
ATOM   3291 C CA  . SER   B 1 71  ? -39.977 18.719  -31.522 1.00 34.42  ? 68  SER   B CA  1 
ATOM   3292 C C   . SER   B 1 71  ? -39.617 17.435  -32.247 1.00 36.25  ? 68  SER   B C   1 
ATOM   3293 O O   . SER   B 1 71  ? -38.474 16.973  -32.208 1.00 40.86  ? 68  SER   B O   1 
ATOM   3294 C CB  . SER   B 1 71  ? -40.052 19.879  -32.527 1.00 33.13  ? 68  SER   B CB  1 
ATOM   3295 O OG  . SER   B 1 71  ? -38.926 19.913  -33.381 1.00 35.96  ? 68  SER   B OG  1 
ATOM   3296 N N   . ILE   B 1 72  ? -40.626 16.856  -32.903 1.00 37.78  ? 69  ILE   B N   1 
ATOM   3297 C CA  . ILE   B 1 72  ? -40.444 15.778  -33.867 1.00 37.73  ? 69  ILE   B CA  1 
ATOM   3298 C C   . ILE   B 1 72  ? -40.664 16.367  -35.252 1.00 34.72  ? 69  ILE   B C   1 
ATOM   3299 O O   . ILE   B 1 72  ? -41.676 17.036  -35.498 1.00 36.93  ? 69  ILE   B O   1 
ATOM   3300 C CB  . ILE   B 1 72  ? -41.400 14.604  -33.601 1.00 37.79  ? 69  ILE   B CB  1 
ATOM   3301 C CG1 . ILE   B 1 72  ? -41.091 13.970  -32.254 1.00 38.35  ? 69  ILE   B CG1 1 
ATOM   3302 C CG2 . ILE   B 1 72  ? -41.292 13.556  -34.712 1.00 38.21  ? 69  ILE   B CG2 1 
ATOM   3303 C CD1 . ILE   B 1 72  ? -42.201 13.085  -31.782 1.00 44.73  ? 69  ILE   B CD1 1 
ATOM   3304 N N   . MET   B 1 73  ? -39.714 16.135  -36.145 1.00 36.53  ? 70  MET   B N   1 
ATOM   3305 C CA  . MET   B 1 73  ? -39.686 16.750  -37.462 1.00 41.18  ? 70  MET   B CA  1 
ATOM   3306 C C   . MET   B 1 73  ? -39.534 15.673  -38.528 1.00 42.17  ? 70  MET   B C   1 
ATOM   3307 O O   . MET   B 1 73  ? -39.247 14.507  -38.236 1.00 40.47  ? 70  MET   B O   1 
ATOM   3308 C CB  . MET   B 1 73  ? -38.543 17.766  -37.568 1.00 37.13  ? 70  MET   B CB  1 
ATOM   3309 C CG  . MET   B 1 73  ? -38.651 18.903  -36.587 1.00 35.10  ? 70  MET   B CG  1 
ATOM   3310 S SD  . MET   B 1 73  ? -37.079 19.749  -36.353 1.00 44.02  ? 70  MET   B SD  1 
ATOM   3311 C CE  . MET   B 1 73  ? -36.269 18.741  -35.098 1.00 36.16  ? 70  MET   B CE  1 
ATOM   3312 N N   . GLN   B 1 74  ? -39.718 16.080  -39.780 1.00 40.56  ? 71  GLN   B N   1 
ATOM   3313 C CA  . GLN   B 1 74  ? -39.627 15.165  -40.906 1.00 40.75  ? 71  GLN   B CA  1 
ATOM   3314 C C   . GLN   B 1 74  ? -38.827 15.834  -42.006 1.00 38.66  ? 71  GLN   B C   1 
ATOM   3315 O O   . GLN   B 1 74  ? -39.133 16.963  -42.398 1.00 38.40  ? 71  GLN   B O   1 
ATOM   3316 C CB  . GLN   B 1 74  ? -41.019 14.774  -41.416 1.00 41.57  ? 71  GLN   B CB  1 
ATOM   3317 C CG  . GLN   B 1 74  ? -41.044 14.203  -42.839 1.00 40.51  ? 71  GLN   B CG  1 
ATOM   3318 C CD  . GLN   B 1 74  ? -42.405 13.628  -43.202 1.00 45.45  ? 71  GLN   B CD  1 
ATOM   3319 O OE1 . GLN   B 1 74  ? -42.722 12.486  -42.868 1.00 48.31  ? 71  GLN   B OE1 1 
ATOM   3320 N NE2 . GLN   B 1 74  ? -43.224 14.427  -43.871 1.00 53.93  ? 71  GLN   B NE2 1 
ATOM   3321 N N   . VAL   B 1 75  ? -37.809 15.142  -42.504 1.00 38.95  ? 72  VAL   B N   1 
ATOM   3322 C CA  . VAL   B 1 75  ? -36.909 15.761  -43.473 1.00 45.83  ? 72  VAL   B CA  1 
ATOM   3323 C C   . VAL   B 1 75  ? -37.633 15.872  -44.816 1.00 48.69  ? 72  VAL   B C   1 
ATOM   3324 O O   . VAL   B 1 75  ? -37.879 14.863  -45.479 1.00 49.62  ? 72  VAL   B O   1 
ATOM   3325 C CB  . VAL   B 1 75  ? -35.606 14.970  -43.605 1.00 44.13  ? 72  VAL   B CB  1 
ATOM   3326 C CG1 . VAL   B 1 75  ? -34.577 15.781  -44.344 1.00 44.84  ? 72  VAL   B CG1 1 
ATOM   3327 C CG2 . VAL   B 1 75  ? -35.116 14.571  -42.229 1.00 44.07  ? 72  VAL   B CG2 1 
ATOM   3328 N N   . LEU   B 1 76  ? -37.972 17.098  -45.225 1.00 46.74  ? 73  LEU   B N   1 
ATOM   3329 C CA  . LEU   B 1 76  ? -38.570 17.295  -46.543 1.00 45.76  ? 73  LEU   B CA  1 
ATOM   3330 C C   . LEU   B 1 76  ? -37.529 17.161  -47.637 1.00 47.69  ? 73  LEU   B C   1 
ATOM   3331 O O   . LEU   B 1 76  ? -37.758 16.501  -48.654 1.00 52.38  ? 73  LEU   B O   1 
ATOM   3332 C CB  . LEU   B 1 76  ? -39.230 18.671  -46.646 1.00 43.24  ? 73  LEU   B CB  1 
ATOM   3333 C CG  . LEU   B 1 76  ? -40.456 18.937  -45.793 1.00 45.24  ? 73  LEU   B CG  1 
ATOM   3334 C CD1 . LEU   B 1 76  ? -41.162 20.175  -46.335 1.00 46.61  ? 73  LEU   B CD1 1 
ATOM   3335 C CD2 . LEU   B 1 76  ? -41.362 17.704  -45.760 1.00 39.12  ? 73  LEU   B CD2 1 
ATOM   3336 N N   . ASP   B 1 77  ? -36.394 17.818  -47.458 1.00 50.18  ? 74  ASP   B N   1 
ATOM   3337 C CA  . ASP   B 1 77  ? -35.358 17.887  -48.469 1.00 46.35  ? 74  ASP   B CA  1 
ATOM   3338 C C   . ASP   B 1 77  ? -34.033 17.899  -47.732 1.00 51.83  ? 74  ASP   B C   1 
ATOM   3339 O O   . ASP   B 1 77  ? -33.975 18.214  -46.538 1.00 52.98  ? 74  ASP   B O   1 
ATOM   3340 C CB  . ASP   B 1 77  ? -35.525 19.132  -49.345 1.00 47.93  ? 74  ASP   B CB  1 
ATOM   3341 C CG  . ASP   B 1 77  ? -34.659 19.092  -50.589 1.00 59.04  ? 74  ASP   B CG  1 
ATOM   3342 O OD1 . ASP   B 1 77  ? -34.069 18.022  -50.869 1.00 60.95  ? 74  ASP   B OD1 1 
ATOM   3343 O OD2 . ASP   B 1 77  ? -34.568 20.132  -51.286 1.00 55.57  ? 74  ASP   B OD2 1 
ATOM   3344 N N   . ALA   B 1 78  ? -32.968 17.530  -48.438 1.00 54.80  ? 75  ALA   B N   1 
ATOM   3345 C CA  . ALA   B 1 78  ? -31.674 17.403  -47.780 1.00 55.34  ? 75  ALA   B CA  1 
ATOM   3346 C C   . ALA   B 1 78  ? -30.581 17.597  -48.811 1.00 56.39  ? 75  ALA   B C   1 
ATOM   3347 O O   . ALA   B 1 78  ? -30.663 17.044  -49.912 1.00 63.31  ? 75  ALA   B O   1 
ATOM   3348 C CB  . ALA   B 1 78  ? -31.534 16.039  -47.088 1.00 53.32  ? 75  ALA   B CB  1 
ATOM   3349 N N   . GLY   B 1 79  ? -29.571 18.385  -48.456 1.00 59.84  ? 76  GLY   B N   1 
ATOM   3350 C CA  . GLY   B 1 79  ? -28.425 18.583  -49.310 1.00 61.75  ? 76  GLY   B CA  1 
ATOM   3351 C C   . GLY   B 1 79  ? -27.609 17.310  -49.431 1.00 66.27  ? 76  GLY   B C   1 
ATOM   3352 O O   . GLY   B 1 79  ? -27.857 16.318  -48.732 1.00 65.11  ? 76  GLY   B O   1 
ATOM   3353 N N   . PRO   B 1 80  ? -26.613 17.316  -50.323 1.00 63.88  ? 77  PRO   B N   1 
ATOM   3354 C CA  . PRO   B 1 80  ? -25.839 16.079  -50.551 1.00 65.44  ? 77  PRO   B CA  1 
ATOM   3355 C C   . PRO   B 1 80  ? -25.206 15.514  -49.284 1.00 66.91  ? 77  PRO   B C   1 
ATOM   3356 O O   . PRO   B 1 80  ? -25.426 14.339  -48.951 1.00 64.07  ? 77  PRO   B O   1 
ATOM   3357 C CB  . PRO   B 1 80  ? -24.794 16.519  -51.587 1.00 66.19  ? 77  PRO   B CB  1 
ATOM   3358 C CG  . PRO   B 1 80  ? -24.705 18.021  -51.437 1.00 69.27  ? 77  PRO   B CG  1 
ATOM   3359 C CD  . PRO   B 1 80  ? -26.091 18.460  -51.091 1.00 66.67  ? 77  PRO   B CD  1 
ATOM   3360 N N   . ASN   B 1 81  ? -24.447 16.327  -48.550 1.00 66.40  ? 78  ASN   B N   1 
ATOM   3361 C CA  . ASN   B 1 81  ? -23.792 15.903  -47.308 1.00 70.24  ? 78  ASN   B CA  1 
ATOM   3362 C C   . ASN   B 1 81  ? -24.642 16.173  -46.074 1.00 64.66  ? 78  ASN   B C   1 
ATOM   3363 O O   . ASN   B 1 81  ? -24.129 16.572  -45.022 1.00 59.93  ? 78  ASN   B O   1 
ATOM   3364 C CB  . ASN   B 1 81  ? -22.434 16.586  -47.197 1.00 69.22  ? 78  ASN   B CB  1 
ATOM   3365 C CG  . ASN   B 1 81  ? -21.561 16.315  -48.403 1.00 71.08  ? 78  ASN   B CG  1 
ATOM   3366 O OD1 . ASN   B 1 81  ? -21.310 17.203  -49.224 1.00 68.13  ? 78  ASN   B OD1 1 
ATOM   3367 N ND2 . ASN   B 1 81  ? -21.109 15.073  -48.528 1.00 70.65  ? 78  ASN   B ND2 1 
ATOM   3368 N N   . ALA   B 1 82  ? -25.950 15.974  -46.185 1.00 65.21  ? 79  ALA   B N   1 
ATOM   3369 C CA  . ALA   B 1 82  ? -26.813 16.093  -45.026 1.00 60.37  ? 79  ALA   B CA  1 
ATOM   3370 C C   . ALA   B 1 82  ? -26.693 14.841  -44.167 1.00 55.93  ? 79  ALA   B C   1 
ATOM   3371 O O   . ALA   B 1 82  ? -26.385 13.759  -44.672 1.00 57.98  ? 79  ALA   B O   1 
ATOM   3372 C CB  . ALA   B 1 82  ? -28.265 16.289  -45.450 1.00 57.32  ? 79  ALA   B CB  1 
ATOM   3373 N N   . PRO   B 1 83  ? -26.924 14.968  -42.862 1.00 51.99  ? 80  PRO   B N   1 
ATOM   3374 C CA  . PRO   B 1 83  ? -26.881 13.803  -41.979 1.00 50.97  ? 80  PRO   B CA  1 
ATOM   3375 C C   . PRO   B 1 83  ? -28.144 12.967  -42.001 1.00 55.12  ? 80  PRO   B C   1 
ATOM   3376 O O   . PRO   B 1 83  ? -28.236 12.002  -41.233 1.00 57.24  ? 80  PRO   B O   1 
ATOM   3377 C CB  . PRO   B 1 83  ? -26.687 14.442  -40.600 1.00 53.11  ? 80  PRO   B CB  1 
ATOM   3378 C CG  . PRO   B 1 83  ? -27.387 15.752  -40.721 1.00 46.73  ? 80  PRO   B CG  1 
ATOM   3379 C CD  . PRO   B 1 83  ? -27.059 16.223  -42.106 1.00 51.51  ? 80  PRO   B CD  1 
ATOM   3380 N N   . PHE   B 1 84  ? -29.116 13.330  -42.817 1.00 56.13  ? 81  PHE   B N   1 
ATOM   3381 C CA  . PHE   B 1 84  ? -30.363 12.589  -42.907 1.00 55.69  ? 81  PHE   B CA  1 
ATOM   3382 C C   . PHE   B 1 84  ? -30.963 12.728  -44.293 1.00 56.31  ? 81  PHE   B C   1 
ATOM   3383 O O   . PHE   B 1 84  ? -30.637 13.651  -45.017 1.00 54.88  ? 81  PHE   B O   1 
ATOM   3384 C CB  . PHE   B 1 84  ? -31.363 13.081  -41.873 1.00 57.51  ? 81  PHE   B CB  1 
ATOM   3385 C CG  . PHE   B 1 84  ? -30.922 12.908  -40.453 1.00 56.47  ? 81  PHE   B CG  1 
ATOM   3386 C CD1 . PHE   B 1 84  ? -30.967 11.669  -39.846 1.00 59.46  ? 81  PHE   B CD1 1 
ATOM   3387 C CD2 . PHE   B 1 84  ? -30.479 13.989  -39.719 1.00 56.78  ? 81  PHE   B CD2 1 
ATOM   3388 C CE1 . PHE   B 1 84  ? -30.564 11.510  -38.538 1.00 54.34  ? 81  PHE   B CE1 1 
ATOM   3389 C CE2 . PHE   B 1 84  ? -30.076 13.839  -38.411 1.00 52.03  ? 81  PHE   B CE2 1 
ATOM   3390 C CZ  . PHE   B 1 84  ? -30.121 12.596  -37.819 1.00 52.06  ? 81  PHE   B CZ  1 
ATOM   3391 N N   . ARG   B 1 85  ? -31.840 11.805  -44.672 1.00 60.99  ? 82  ARG   B N   1 
ATOM   3392 C CA  . ARG   B 1 85  ? -32.391 11.851  -46.019 1.00 58.18  ? 82  ARG   B CA  1 
ATOM   3393 C C   . ARG   B 1 85  ? -33.880 12.183  -45.983 1.00 55.52  ? 82  ARG   B C   1 
ATOM   3394 O O   . ARG   B 1 85  ? -34.560 11.926  -44.976 1.00 47.02  ? 82  ARG   B O   1 
ATOM   3395 C CB  . ARG   B 1 85  ? -32.176 10.523  -46.767 1.00 60.60  ? 82  ARG   B CB  1 
ATOM   3396 C CG  . ARG   B 1 85  ? -30.720 10.061  -46.867 1.00 59.97  ? 82  ARG   B CG  1 
ATOM   3397 C CD  . ARG   B 1 85  ? -29.766 11.222  -47.175 1.00 61.27  ? 82  ARG   B CD  1 
ATOM   3398 N NE  . ARG   B 1 85  ? -30.164 11.966  -48.367 1.00 68.54  ? 82  ARG   B NE  1 
ATOM   3399 C CZ  . ARG   B 1 85  ? -29.619 13.111  -48.762 1.00 66.30  ? 82  ARG   B CZ  1 
ATOM   3400 N NH1 . ARG   B 1 85  ? -28.657 13.697  -48.063 1.00 60.90  ? 82  ARG   B NH1 1 
ATOM   3401 N NH2 . ARG   B 1 85  ? -30.047 13.678  -49.892 1.00 61.32  ? 82  ARG   B NH2 1 
ATOM   3402 N N   . PRO   B 1 86  ? -34.405 12.773  -47.065 1.00 53.23  ? 83  PRO   B N   1 
ATOM   3403 C CA  . PRO   B 1 86  ? -35.832 13.104  -47.118 1.00 47.32  ? 83  PRO   B CA  1 
ATOM   3404 C C   . PRO   B 1 86  ? -36.691 11.925  -46.704 1.00 49.68  ? 83  PRO   B C   1 
ATOM   3405 O O   . PRO   B 1 86  ? -36.402 10.775  -47.035 1.00 53.04  ? 83  PRO   B O   1 
ATOM   3406 C CB  . PRO   B 1 86  ? -36.047 13.476  -48.585 1.00 47.98  ? 83  PRO   B CB  1 
ATOM   3407 C CG  . PRO   B 1 86  ? -34.751 14.100  -48.973 1.00 49.49  ? 83  PRO   B CG  1 
ATOM   3408 C CD  . PRO   B 1 86  ? -33.681 13.318  -48.228 1.00 53.22  ? 83  PRO   B CD  1 
ATOM   3409 N N   . GLY   B 1 87  ? -37.738 12.226  -45.941 1.00 49.65  ? 84  GLY   B N   1 
ATOM   3410 C CA  . GLY   B 1 87  ? -38.573 11.222  -45.338 1.00 41.96  ? 84  GLY   B CA  1 
ATOM   3411 C C   . GLY   B 1 87  ? -38.129 10.776  -43.964 1.00 53.09  ? 84  GLY   B C   1 
ATOM   3412 O O   . GLY   B 1 87  ? -38.944 10.213  -43.220 1.00 52.31  ? 84  GLY   B O   1 
ATOM   3413 N N   . ASP   B 1 88  ? -36.864 11.017  -43.599 1.00 55.15  ? 85  ASP   B N   1 
ATOM   3414 C CA  . ASP   B 1 88  ? -36.396 10.644  -42.270 1.00 51.51  ? 85  ASP   B CA  1 
ATOM   3415 C C   . ASP   B 1 88  ? -37.162 11.411  -41.198 1.00 52.00  ? 85  ASP   B C   1 
ATOM   3416 O O   . ASP   B 1 88  ? -37.496 12.588  -41.370 1.00 52.50  ? 85  ASP   B O   1 
ATOM   3417 C CB  . ASP   B 1 88  ? -34.893 10.912  -42.129 1.00 55.57  ? 85  ASP   B CB  1 
ATOM   3418 C CG  . ASP   B 1 88  ? -34.033 9.867   -42.845 1.00 62.48  ? 85  ASP   B CG  1 
ATOM   3419 O OD1 . ASP   B 1 88  ? -34.433 8.679   -42.872 1.00 61.81  ? 85  ASP   B OD1 1 
ATOM   3420 O OD2 . ASP   B 1 88  ? -32.956 10.233  -43.374 1.00 55.14  ? 85  ASP   B OD2 1 
ATOM   3421 N N   . LEU   B 1 89  ? -37.452 10.731  -40.092 1.00 52.55  ? 86  LEU   B N   1 
ATOM   3422 C CA  . LEU   B 1 89  ? -38.065 11.346  -38.923 1.00 49.95  ? 86  LEU   B CA  1 
ATOM   3423 C C   . LEU   B 1 89  ? -36.990 11.578  -37.870 1.00 55.70  ? 86  LEU   B C   1 
ATOM   3424 O O   . LEU   B 1 89  ? -36.194 10.676  -37.584 1.00 55.71  ? 86  LEU   B O   1 
ATOM   3425 C CB  . LEU   B 1 89  ? -39.183 10.469  -38.360 1.00 47.63  ? 86  LEU   B CB  1 
ATOM   3426 C CG  . LEU   B 1 89  ? -40.442 10.360  -39.221 1.00 48.90  ? 86  LEU   B CG  1 
ATOM   3427 C CD1 . LEU   B 1 89  ? -41.602 9.958   -38.359 1.00 44.71  ? 86  LEU   B CD1 1 
ATOM   3428 C CD2 . LEU   B 1 89  ? -40.745 11.676  -39.887 1.00 49.02  ? 86  LEU   B CD2 1 
ATOM   3429 N N   . VAL   B 1 90  ? -36.953 12.790  -37.306 1.00 52.92  ? 87  VAL   B N   1 
ATOM   3430 C CA  . VAL   B 1 90  ? -35.925 13.155  -36.340 1.00 48.30  ? 87  VAL   B CA  1 
ATOM   3431 C C   . VAL   B 1 90  ? -36.548 13.880  -35.156 1.00 43.34  ? 87  VAL   B C   1 
ATOM   3432 O O   . VAL   B 1 90  ? -37.645 14.431  -35.235 1.00 44.45  ? 87  VAL   B O   1 
ATOM   3433 C CB  . VAL   B 1 90  ? -34.825 14.029  -36.970 1.00 45.65  ? 87  VAL   B CB  1 
ATOM   3434 C CG1 . VAL   B 1 90  ? -34.218 13.327  -38.173 1.00 53.58  ? 87  VAL   B CG1 1 
ATOM   3435 C CG2 . VAL   B 1 90  ? -35.389 15.383  -37.352 1.00 44.59  ? 87  VAL   B CG2 1 
ATOM   3436 N N   . GLN   B 1 91  ? -35.830 13.855  -34.041 1.00 44.62  ? 88  GLN   B N   1 
ATOM   3437 C CA  . GLN   B 1 91  ? -36.201 14.579  -32.833 1.00 44.68  ? 88  GLN   B CA  1 
ATOM   3438 C C   . GLN   B 1 91  ? -35.073 15.544  -32.484 1.00 42.67  ? 88  GLN   B C   1 
ATOM   3439 O O   . GLN   B 1 91  ? -33.888 15.186  -32.539 1.00 44.37  ? 88  GLN   B O   1 
ATOM   3440 C CB  . GLN   B 1 91  ? -36.487 13.607  -31.674 1.00 41.05  ? 88  GLN   B CB  1 
ATOM   3441 C CG  . GLN   B 1 91  ? -36.773 14.262  -30.320 1.00 42.08  ? 88  GLN   B CG  1 
ATOM   3442 C CD  . GLN   B 1 91  ? -35.511 14.455  -29.475 1.00 48.59  ? 88  GLN   B CD  1 
ATOM   3443 O OE1 . GLN   B 1 91  ? -34.704 13.529  -29.302 1.00 50.94  ? 88  GLN   B OE1 1 
ATOM   3444 N NE2 . GLN   B 1 91  ? -35.330 15.668  -28.956 1.00 45.47  ? 88  GLN   B NE2 1 
ATOM   3445 N N   . GLY   B 1 92  ? -35.445 16.773  -32.155 1.00 39.06  ? 89  GLY   B N   1 
ATOM   3446 C CA  . GLY   B 1 92  ? -34.463 17.814  -31.916 1.00 36.55  ? 89  GLY   B CA  1 
ATOM   3447 C C   . GLY   B 1 92  ? -35.163 19.043  -31.390 1.00 36.46  ? 89  GLY   B C   1 
ATOM   3448 O O   . GLY   B 1 92  ? -36.374 19.040  -31.160 1.00 34.78  ? 89  GLY   B O   1 
ATOM   3449 N N   . PHE   B 1 93  ? -34.372 20.097  -31.176 1.00 36.82  ? 90  PHE   B N   1 
ATOM   3450 C CA  . PHE   B 1 93  ? -34.871 21.346  -30.600 1.00 30.23  ? 90  PHE   B CA  1 
ATOM   3451 C C   . PHE   B 1 93  ? -35.325 22.284  -31.721 1.00 34.19  ? 90  PHE   B C   1 
ATOM   3452 O O   . PHE   B 1 93  ? -34.791 23.377  -31.929 1.00 36.45  ? 90  PHE   B O   1 
ATOM   3453 C CB  . PHE   B 1 93  ? -33.798 21.984  -29.724 1.00 32.07  ? 90  PHE   B CB  1 
ATOM   3454 C CG  . PHE   B 1 93  ? -34.337 22.809  -28.570 1.00 30.13  ? 90  PHE   B CG  1 
ATOM   3455 C CD1 . PHE   B 1 93  ? -34.998 22.203  -27.506 1.00 27.61  ? 90  PHE   B CD1 1 
ATOM   3456 C CD2 . PHE   B 1 93  ? -34.141 24.183  -28.529 1.00 29.68  ? 90  PHE   B CD2 1 
ATOM   3457 C CE1 . PHE   B 1 93  ? -35.482 22.944  -26.433 1.00 27.11  ? 90  PHE   B CE1 1 
ATOM   3458 C CE2 . PHE   B 1 93  ? -34.615 24.938  -27.445 1.00 30.88  ? 90  PHE   B CE2 1 
ATOM   3459 C CZ  . PHE   B 1 93  ? -35.295 24.309  -26.401 1.00 28.86  ? 90  PHE   B CZ  1 
ATOM   3460 N N   . GLY   B 1 94  ? -36.334 21.820  -32.464 1.00 33.21  ? 91  GLY   B N   1 
ATOM   3461 C CA  . GLY   B 1 94  ? -36.776 22.551  -33.638 1.00 35.26  ? 91  GLY   B CA  1 
ATOM   3462 C C   . GLY   B 1 94  ? -37.471 23.856  -33.315 1.00 30.22  ? 91  GLY   B C   1 
ATOM   3463 O O   . GLY   B 1 94  ? -37.395 24.806  -34.097 1.00 31.11  ? 91  GLY   B O   1 
ATOM   3464 N N   . GLY   B 1 95  ? -38.148 23.923  -32.172 1.00 28.75  ? 92  GLY   B N   1 
ATOM   3465 C CA  . GLY   B 1 95  ? -38.863 25.117  -31.757 1.00 28.49  ? 92  GLY   B CA  1 
ATOM   3466 C C   . GLY   B 1 95  ? -40.277 25.193  -32.304 1.00 32.04  ? 92  GLY   B C   1 
ATOM   3467 O O   . GLY   B 1 95  ? -40.734 24.358  -33.094 1.00 30.09  ? 92  GLY   B O   1 
ATOM   3468 N N   . TRP   B 1 96  ? -40.982 26.248  -31.872 1.00 31.05  ? 93  TRP   B N   1 
ATOM   3469 C CA  . TRP   B 1 96  ? -42.356 26.537  -32.301 1.00 27.45  ? 93  TRP   B CA  1 
ATOM   3470 C C   . TRP   B 1 96  ? -42.349 27.180  -33.698 1.00 29.38  ? 93  TRP   B C   1 
ATOM   3471 O O   . TRP   B 1 96  ? -42.627 28.365  -33.886 1.00 30.64  ? 93  TRP   B O   1 
ATOM   3472 C CB  . TRP   B 1 96  ? -43.047 27.436  -31.280 1.00 23.97  ? 93  TRP   B CB  1 
ATOM   3473 C CG  . TRP   B 1 96  ? -43.216 26.832  -29.911 1.00 28.35  ? 93  TRP   B CG  1 
ATOM   3474 C CD1 . TRP   B 1 96  ? -42.964 25.535  -29.540 1.00 28.93  ? 93  TRP   B CD1 1 
ATOM   3475 C CD2 . TRP   B 1 96  ? -43.667 27.503  -28.724 1.00 28.98  ? 93  TRP   B CD2 1 
ATOM   3476 N NE1 . TRP   B 1 96  ? -43.241 25.357  -28.203 1.00 27.48  ? 93  TRP   B NE1 1 
ATOM   3477 C CE2 . TRP   B 1 96  ? -43.669 26.549  -27.676 1.00 29.88  ? 93  TRP   B CE2 1 
ATOM   3478 C CE3 . TRP   B 1 96  ? -44.074 28.811  -28.447 1.00 26.30  ? 93  TRP   B CE3 1 
ATOM   3479 C CZ2 . TRP   B 1 96  ? -44.060 26.869  -26.370 1.00 29.12  ? 93  TRP   B CZ2 1 
ATOM   3480 C CZ3 . TRP   B 1 96  ? -44.462 29.129  -27.158 1.00 29.75  ? 93  TRP   B CZ3 1 
ATOM   3481 C CH2 . TRP   B 1 96  ? -44.454 28.156  -26.128 1.00 31.36  ? 93  TRP   B CH2 1 
ATOM   3482 N N   . ARG   B 1 97  ? -42.003 26.368  -34.700 1.00 31.34  ? 94  ARG   B N   1 
ATOM   3483 C CA  . ARG   B 1 97  ? -41.992 26.773  -36.103 1.00 29.36  ? 94  ARG   B CA  1 
ATOM   3484 C C   . ARG   B 1 97  ? -42.623 25.649  -36.904 1.00 30.45  ? 94  ARG   B C   1 
ATOM   3485 O O   . ARG   B 1 97  ? -42.409 24.480  -36.578 1.00 31.71  ? 94  ARG   B O   1 
ATOM   3486 C CB  . ARG   B 1 97  ? -40.567 27.035  -36.596 1.00 30.00  ? 94  ARG   B CB  1 
ATOM   3487 C CG  . ARG   B 1 97  ? -39.812 28.097  -35.794 1.00 33.53  ? 94  ARG   B CG  1 
ATOM   3488 C CD  . ARG   B 1 97  ? -38.384 28.288  -36.296 1.00 31.71  ? 94  ARG   B CD  1 
ATOM   3489 N NE  . ARG   B 1 97  ? -37.501 27.227  -35.831 1.00 33.62  ? 94  ARG   B NE  1 
ATOM   3490 C CZ  . ARG   B 1 97  ? -36.235 27.071  -36.201 1.00 35.12  ? 94  ARG   B CZ  1 
ATOM   3491 N NH1 . ARG   B 1 97  ? -35.658 27.890  -37.070 1.00 32.19  ? 94  ARG   B NH1 1 
ATOM   3492 N NH2 . ARG   B 1 97  ? -35.528 26.070  -35.682 1.00 33.99  ? 94  ARG   B NH2 1 
ATOM   3493 N N   . THR   B 1 98  ? -43.420 25.980  -37.932 1.00 30.34  ? 95  THR   B N   1 
ATOM   3494 C CA  . THR   B 1 98  ? -43.991 24.910  -38.756 1.00 29.18  ? 95  THR   B CA  1 
ATOM   3495 C C   . THR   B 1 98  ? -42.937 24.275  -39.659 1.00 32.04  ? 95  THR   B C   1 
ATOM   3496 O O   . THR   B 1 98  ? -43.043 23.087  -39.985 1.00 32.21  ? 95  THR   B O   1 
ATOM   3497 C CB  . THR   B 1 98  ? -45.160 25.419  -39.606 1.00 29.86  ? 95  THR   B CB  1 
ATOM   3498 O OG1 . THR   B 1 98  ? -44.669 26.300  -40.630 1.00 32.38  ? 95  THR   B OG1 1 
ATOM   3499 C CG2 . THR   B 1 98  ? -46.184 26.151  -38.742 1.00 26.97  ? 95  THR   B CG2 1 
ATOM   3500 N N   . HIS   B 1 99  ? -41.917 25.039  -40.062 1.00 28.24  ? 96  HIS   B N   1 
ATOM   3501 C CA  . HIS   B 1 99  ? -40.834 24.546  -40.898 1.00 30.13  ? 96  HIS   B CA  1 
ATOM   3502 C C   . HIS   B 1 99  ? -39.564 25.306  -40.534 1.00 34.60  ? 96  HIS   B C   1 
ATOM   3503 O O   . HIS   B 1 99  ? -39.621 26.412  -39.986 1.00 32.39  ? 96  HIS   B O   1 
ATOM   3504 C CB  . HIS   B 1 99  ? -41.115 24.739  -42.399 1.00 33.94  ? 96  HIS   B CB  1 
ATOM   3505 C CG  . HIS   B 1 99  ? -42.420 24.173  -42.869 1.00 36.38  ? 96  HIS   B CG  1 
ATOM   3506 N ND1 . HIS   B 1 99  ? -43.630 24.803  -42.653 1.00 35.75  ? 96  HIS   B ND1 1 
ATOM   3507 C CD2 . HIS   B 1 99  ? -42.700 23.055  -43.584 1.00 37.47  ? 96  HIS   B CD2 1 
ATOM   3508 C CE1 . HIS   B 1 99  ? -44.598 24.078  -43.188 1.00 37.01  ? 96  HIS   B CE1 1 
ATOM   3509 N NE2 . HIS   B 1 99  ? -44.059 23.019  -43.768 1.00 36.92  ? 96  HIS   B NE2 1 
ATOM   3510 N N   . LEU   B 1 100 ? -38.416 24.726  -40.894 1.00 34.22  ? 97  LEU   B N   1 
ATOM   3511 C CA  . LEU   B 1 100 ? -37.112 25.298  -40.574 1.00 32.98  ? 97  LEU   B CA  1 
ATOM   3512 C C   . LEU   B 1 100 ? -36.038 24.623  -41.411 1.00 34.58  ? 97  LEU   B C   1 
ATOM   3513 O O   . LEU   B 1 100 ? -36.198 23.485  -41.854 1.00 38.15  ? 97  LEU   B O   1 
ATOM   3514 C CB  . LEU   B 1 100 ? -36.764 25.132  -39.096 1.00 30.16  ? 97  LEU   B CB  1 
ATOM   3515 C CG  . LEU   B 1 100 ? -36.609 23.678  -38.665 1.00 34.91  ? 97  LEU   B CG  1 
ATOM   3516 C CD1 . LEU   B 1 100 ? -35.410 23.499  -37.761 1.00 38.70  ? 97  LEU   B CD1 1 
ATOM   3517 C CD2 . LEU   B 1 100 ? -37.854 23.274  -37.926 1.00 35.78  ? 97  LEU   B CD2 1 
ATOM   3518 N N   . VAL   B 1 101 ? -34.925 25.329  -41.596 1.00 35.95  ? 98  VAL   B N   1 
ATOM   3519 C CA  . VAL   B 1 101 ? -33.717 24.777  -42.202 1.00 36.40  ? 98  VAL   B CA  1 
ATOM   3520 C C   . VAL   B 1 101 ? -32.663 24.633  -41.109 1.00 37.20  ? 98  VAL   B C   1 
ATOM   3521 O O   . VAL   B 1 101 ? -32.303 25.616  -40.455 1.00 39.52  ? 98  VAL   B O   1 
ATOM   3522 C CB  . VAL   B 1 101 ? -33.198 25.663  -43.343 1.00 39.69  ? 98  VAL   B CB  1 
ATOM   3523 C CG1 . VAL   B 1 101 ? -31.834 25.168  -43.825 1.00 37.60  ? 98  VAL   B CG1 1 
ATOM   3524 C CG2 . VAL   B 1 101 ? -34.208 25.716  -44.493 1.00 37.79  ? 98  VAL   B CG2 1 
ATOM   3525 N N   . SER   B 1 102 ? -32.158 23.418  -40.911 1.00 39.68  ? 99  SER   B N   1 
ATOM   3526 C CA  . SER   B 1 102 ? -31.065 23.191  -39.975 1.00 42.41  ? 99  SER   B CA  1 
ATOM   3527 C C   . SER   B 1 102 ? -30.106 22.155  -40.545 1.00 48.56  ? 99  SER   B C   1 
ATOM   3528 O O   . SER   B 1 102 ? -30.475 21.331  -41.391 1.00 43.74  ? 99  SER   B O   1 
ATOM   3529 C CB  . SER   B 1 102 ? -31.569 22.719  -38.598 1.00 39.31  ? 99  SER   B CB  1 
ATOM   3530 O OG  . SER   B 1 102 ? -30.520 22.103  -37.865 1.00 40.74  ? 99  SER   B OG  1 
ATOM   3531 N N   . ASP   B 1 103 ? -28.864 22.191  -40.062 1.00 47.89  ? 100 ASP   B N   1 
ATOM   3532 C CA  . ASP   B 1 103 ? -27.959 21.086  -40.335 1.00 45.39  ? 100 ASP   B CA  1 
ATOM   3533 C C   . ASP   B 1 103 ? -27.994 20.030  -39.243 1.00 41.28  ? 100 ASP   B C   1 
ATOM   3534 O O   . ASP   B 1 103 ? -27.352 18.989  -39.387 1.00 42.55  ? 100 ASP   B O   1 
ATOM   3535 C CB  . ASP   B 1 103 ? -26.533 21.588  -40.555 1.00 49.84  ? 100 ASP   B CB  1 
ATOM   3536 C CG  . ASP   B 1 103 ? -25.985 22.357  -39.374 1.00 55.56  ? 100 ASP   B CG  1 
ATOM   3537 O OD1 . ASP   B 1 103 ? -26.621 22.367  -38.295 1.00 57.87  ? 100 ASP   B OD1 1 
ATOM   3538 O OD2 . ASP   B 1 103 ? -24.901 22.960  -39.536 1.00 57.78  ? 100 ASP   B OD2 1 
ATOM   3539 N N   . GLY   B 1 104 ? -28.755 20.256  -38.175 1.00 39.42  ? 101 GLY   B N   1 
ATOM   3540 C CA  . GLY   B 1 104 ? -28.949 19.242  -37.161 1.00 44.74  ? 101 GLY   B CA  1 
ATOM   3541 C C   . GLY   B 1 104 ? -27.756 18.974  -36.263 1.00 47.10  ? 101 GLY   B C   1 
ATOM   3542 O O   . GLY   B 1 104 ? -27.847 18.106  -35.383 1.00 42.87  ? 101 GLY   B O   1 
ATOM   3543 N N   . LYS   B 1 105 ? -26.644 19.681  -36.456 1.00 43.26  ? 102 LYS   B N   1 
ATOM   3544 C CA  . LYS   B 1 105 ? -25.477 19.487  -35.624 1.00 45.09  ? 102 LYS   B CA  1 
ATOM   3545 C C   . LYS   B 1 105 ? -25.730 20.121  -34.257 1.00 46.27  ? 102 LYS   B C   1 
ATOM   3546 O O   . LYS   B 1 105 ? -26.637 20.946  -34.114 1.00 45.16  ? 102 LYS   B O   1 
ATOM   3547 C CB  . LYS   B 1 105 ? -24.253 20.083  -36.317 1.00 43.44  ? 102 LYS   B CB  1 
ATOM   3548 C CG  . LYS   B 1 105 ? -23.962 19.440  -37.658 1.00 44.76  ? 102 LYS   B CG  1 
ATOM   3549 C CD  . LYS   B 1 105 ? -22.545 19.716  -38.138 1.00 51.26  ? 102 LYS   B CD  1 
ATOM   3550 C CE  . LYS   B 1 105 ? -22.492 20.914  -39.056 1.00 56.82  ? 102 LYS   B CE  1 
ATOM   3551 N NZ  . LYS   B 1 105 ? -21.713 20.607  -40.285 1.00 60.19  ? 102 LYS   B NZ  1 
ATOM   3552 N N   . PRO   B 1 106 ? -24.969 19.736  -33.225 1.00 44.97  ? 103 PRO   B N   1 
ATOM   3553 C CA  . PRO   B 1 106 ? -25.229 20.291  -31.894 1.00 40.66  ? 103 PRO   B CA  1 
ATOM   3554 C C   . PRO   B 1 106 ? -24.963 21.784  -31.903 1.00 38.67  ? 103 PRO   B C   1 
ATOM   3555 O O   . PRO   B 1 106 ? -24.118 22.275  -32.647 1.00 41.60  ? 103 PRO   B O   1 
ATOM   3556 C CB  . PRO   B 1 106 ? -24.244 19.546  -30.987 1.00 37.13  ? 103 PRO   B CB  1 
ATOM   3557 C CG  . PRO   B 1 106 ? -23.684 18.442  -31.814 1.00 40.76  ? 103 PRO   B CG  1 
ATOM   3558 C CD  . PRO   B 1 106 ? -23.735 18.937  -33.224 1.00 38.88  ? 103 PRO   B CD  1 
ATOM   3559 N N   . LYS   B 1 107 ? -25.713 22.513  -31.085 1.00 44.70  ? 104 LYS   B N   1 
ATOM   3560 C CA  . LYS   B 1 107 ? -25.741 23.962  -31.194 1.00 43.24  ? 104 LYS   B CA  1 
ATOM   3561 C C   . LYS   B 1 107 ? -25.660 24.584  -29.817 1.00 41.06  ? 104 LYS   B C   1 
ATOM   3562 O O   . LYS   B 1 107 ? -26.328 24.139  -28.876 1.00 41.40  ? 104 LYS   B O   1 
ATOM   3563 C CB  . LYS   B 1 107 ? -27.006 24.445  -31.905 1.00 43.94  ? 104 LYS   B CB  1 
ATOM   3564 C CG  . LYS   B 1 107 ? -26.798 25.697  -32.728 1.00 49.00  ? 104 LYS   B CG  1 
ATOM   3565 C CD  . LYS   B 1 107 ? -27.406 25.540  -34.118 1.00 56.22  ? 104 LYS   B CD  1 
ATOM   3566 C CE  . LYS   B 1 107 ? -26.677 24.460  -34.948 1.00 55.82  ? 104 LYS   B CE  1 
ATOM   3567 N NZ  . LYS   B 1 107 ? -27.120 24.411  -36.386 1.00 55.63  ? 104 LYS   B NZ  1 
ATOM   3568 N N   . LEU   B 1 108 ? -24.848 25.627  -29.720 1.00 45.28  ? 105 LEU   B N   1 
ATOM   3569 C CA  . LEU   B 1 108 ? -24.599 26.291  -28.453 1.00 42.64  ? 105 LEU   B CA  1 
ATOM   3570 C C   . LEU   B 1 108 ? -25.689 27.323  -28.183 1.00 40.09  ? 105 LEU   B C   1 
ATOM   3571 O O   . LEU   B 1 108 ? -25.997 28.150  -29.043 1.00 41.25  ? 105 LEU   B O   1 
ATOM   3572 C CB  . LEU   B 1 108 ? -23.219 26.947  -28.479 1.00 42.47  ? 105 LEU   B CB  1 
ATOM   3573 C CG  . LEU   B 1 108 ? -22.955 27.983  -27.385 1.00 47.70  ? 105 LEU   B CG  1 
ATOM   3574 C CD1 . LEU   B 1 108 ? -22.917 27.342  -26.006 1.00 41.85  ? 105 LEU   B CD1 1 
ATOM   3575 C CD2 . LEU   B 1 108 ? -21.683 28.735  -27.684 1.00 45.05  ? 105 LEU   B CD2 1 
ATOM   3576 N N   . TRP   B 1 109 ? -26.265 27.277  -26.984 1.00 38.27  ? 106 TRP   B N   1 
ATOM   3577 C CA  . TRP   B 1 109 ? -27.295 28.228  -26.570 1.00 38.45  ? 106 TRP   B CA  1 
ATOM   3578 C C   . TRP   B 1 109 ? -26.599 29.489  -26.042 1.00 41.55  ? 106 TRP   B C   1 
ATOM   3579 O O   . TRP   B 1 109 ? -26.354 29.650  -24.844 1.00 41.70  ? 106 TRP   B O   1 
ATOM   3580 C CB  . TRP   B 1 109 ? -28.219 27.578  -25.544 1.00 36.02  ? 106 TRP   B CB  1 
ATOM   3581 C CG  . TRP   B 1 109 ? -29.303 28.461  -25.034 1.00 35.75  ? 106 TRP   B CG  1 
ATOM   3582 C CD1 . TRP   B 1 109 ? -29.612 28.707  -23.721 1.00 38.32  ? 106 TRP   B CD1 1 
ATOM   3583 C CD2 . TRP   B 1 109 ? -30.218 29.232  -25.812 1.00 35.94  ? 106 TRP   B CD2 1 
ATOM   3584 N NE1 . TRP   B 1 109 ? -30.666 29.579  -23.638 1.00 33.24  ? 106 TRP   B NE1 1 
ATOM   3585 C CE2 . TRP   B 1 109 ? -31.060 29.918  -24.905 1.00 36.13  ? 106 TRP   B CE2 1 
ATOM   3586 C CE3 . TRP   B 1 109 ? -30.417 29.409  -27.185 1.00 34.49  ? 106 TRP   B CE3 1 
ATOM   3587 C CZ2 . TRP   B 1 109 ? -32.078 30.776  -25.332 1.00 35.44  ? 106 TRP   B CZ2 1 
ATOM   3588 C CZ3 . TRP   B 1 109 ? -31.423 30.269  -27.604 1.00 29.57  ? 106 TRP   B CZ3 1 
ATOM   3589 C CH2 . TRP   B 1 109 ? -32.245 30.933  -26.681 1.00 29.53  ? 106 TRP   B CH2 1 
ATOM   3590 N N   . GLN   B 1 110 ? -26.311 30.415  -26.964 1.00 43.08  ? 107 GLN   B N   1 
ATOM   3591 C CA  . GLN   B 1 110 ? -25.380 31.522  -26.750 1.00 40.35  ? 107 GLN   B CA  1 
ATOM   3592 C C   . GLN   B 1 110 ? -25.890 32.594  -25.799 1.00 40.76  ? 107 GLN   B C   1 
ATOM   3593 O O   . GLN   B 1 110 ? -25.104 33.453  -25.385 1.00 37.96  ? 107 GLN   B O   1 
ATOM   3594 C CB  . GLN   B 1 110 ? -25.059 32.177  -28.084 1.00 43.85  ? 107 GLN   B CB  1 
ATOM   3595 C CG  . GLN   B 1 110 ? -24.846 31.195  -29.215 1.00 45.29  ? 107 GLN   B CG  1 
ATOM   3596 C CD  . GLN   B 1 110 ? -24.874 31.879  -30.555 1.00 58.57  ? 107 GLN   B CD  1 
ATOM   3597 O OE1 . GLN   B 1 110 ? -25.683 31.542  -31.421 1.00 71.86  ? 107 GLN   B OE1 1 
ATOM   3598 N NE2 . GLN   B 1 110 ? -23.997 32.859  -30.734 1.00 63.11  ? 107 GLN   B NE2 1 
ATOM   3599 N N   . THR   B 1 111 ? -27.174 32.592  -25.465 1.00 39.99  ? 108 THR   B N   1 
ATOM   3600 C CA  . THR   B 1 111 ? -27.749 33.638  -24.635 1.00 36.27  ? 108 THR   B CA  1 
ATOM   3601 C C   . THR   B 1 111 ? -28.209 33.110  -23.290 1.00 36.11  ? 108 THR   B C   1 
ATOM   3602 O O   . THR   B 1 111 ? -28.773 33.875  -22.502 1.00 37.63  ? 108 THR   B O   1 
ATOM   3603 C CB  . THR   B 1 111 ? -28.926 34.322  -25.362 1.00 35.88  ? 108 THR   B CB  1 
ATOM   3604 O OG1 . THR   B 1 111 ? -29.898 33.335  -25.750 1.00 34.58  ? 108 THR   B OG1 1 
ATOM   3605 C CG2 . THR   B 1 111 ? -28.450 35.087  -26.622 1.00 27.49  ? 108 THR   B CG2 1 
ATOM   3606 N N   . GLY   B 1 112 ? -27.980 31.825  -23.004 1.00 36.63  ? 109 GLY   B N   1 
ATOM   3607 C CA  . GLY   B 1 112 ? -28.482 31.242  -21.781 1.00 40.01  ? 109 GLY   B CA  1 
ATOM   3608 C C   . GLY   B 1 112 ? -27.681 31.615  -20.540 1.00 43.31  ? 109 GLY   B C   1 
ATOM   3609 O O   . GLY   B 1 112 ? -26.581 32.167  -20.584 1.00 43.28  ? 109 GLY   B O   1 
ATOM   3610 N N   . THR   B 1 113 ? -28.260 31.292  -19.387 1.00 42.42  ? 110 THR   B N   1 
ATOM   3611 C CA  . THR   B 1 113 ? -27.526 31.458  -18.139 1.00 42.50  ? 110 THR   B CA  1 
ATOM   3612 C C   . THR   B 1 113 ? -26.236 30.637  -18.147 1.00 43.38  ? 110 THR   B C   1 
ATOM   3613 O O   . THR   B 1 113 ? -25.171 31.131  -17.758 1.00 45.15  ? 110 THR   B O   1 
ATOM   3614 C CB  . THR   B 1 113 ? -28.433 31.068  -16.975 1.00 48.89  ? 110 THR   B CB  1 
ATOM   3615 O OG1 . THR   B 1 113 ? -29.631 31.860  -17.022 1.00 44.55  ? 110 THR   B OG1 1 
ATOM   3616 C CG2 . THR   B 1 113 ? -27.726 31.259  -15.635 1.00 38.69  ? 110 THR   B CG2 1 
ATOM   3617 N N   . PHE   B 1 114 ? -26.347 29.397  -18.594 1.00 43.77  ? 111 PHE   B N   1 
ATOM   3618 C CA  . PHE   B 1 114 ? -25.240 28.473  -18.622 1.00 40.79  ? 111 PHE   B CA  1 
ATOM   3619 C C   . PHE   B 1 114 ? -24.823 28.122  -20.029 1.00 43.11  ? 111 PHE   B C   1 
ATOM   3620 O O   . PHE   B 1 114 ? -25.543 28.406  -20.968 1.00 44.65  ? 111 PHE   B O   1 
ATOM   3621 C CB  . PHE   B 1 114 ? -25.708 27.179  -17.976 1.00 37.19  ? 111 PHE   B CB  1 
ATOM   3622 C CG  . PHE   B 1 114 ? -25.976 27.276  -16.514 1.00 42.74  ? 111 PHE   B CG  1 
ATOM   3623 C CD1 . PHE   B 1 114 ? -24.938 27.321  -15.610 1.00 41.14  ? 111 PHE   B CD1 1 
ATOM   3624 C CD2 . PHE   B 1 114 ? -27.270 27.273  -16.041 1.00 41.34  ? 111 PHE   B CD2 1 
ATOM   3625 C CE1 . PHE   B 1 114 ? -25.186 27.388  -14.256 1.00 36.69  ? 111 PHE   B CE1 1 
ATOM   3626 C CE2 . PHE   B 1 114 ? -27.525 27.342  -14.691 1.00 39.15  ? 111 PHE   B CE2 1 
ATOM   3627 C CZ  . PHE   B 1 114 ? -26.481 27.398  -13.797 1.00 34.91  ? 111 PHE   B CZ  1 
ATOM   3628 N N   . PRO   B 1 115 ? -23.669 27.475  -20.180 1.00 41.05  ? 112 PRO   B N   1 
ATOM   3629 C CA  . PRO   B 1 115 ? -23.164 27.068  -21.492 1.00 40.29  ? 112 PRO   B CA  1 
ATOM   3630 C C   . PRO   B 1 115 ? -23.787 25.800  -22.045 1.00 40.47  ? 112 PRO   B C   1 
ATOM   3631 O O   . PRO   B 1 115 ? -23.079 24.852  -22.300 1.00 41.76  ? 112 PRO   B O   1 
ATOM   3632 C CB  . PRO   B 1 115 ? -21.696 26.812  -21.202 1.00 41.07  ? 112 PRO   B CB  1 
ATOM   3633 C CG  . PRO   B 1 115 ? -21.634 26.462  -19.766 1.00 40.45  ? 112 PRO   B CG  1 
ATOM   3634 C CD  . PRO   B 1 115 ? -22.643 27.356  -19.135 1.00 38.99  ? 112 PRO   B CD  1 
ATOM   3635 N N   . MET   B 1 116 ? -25.087 25.801  -22.262 1.00 41.10  ? 113 MET   B N   1 
ATOM   3636 C CA  . MET   B 1 116 ? -25.790 24.632  -22.760 1.00 39.92  ? 113 MET   B CA  1 
ATOM   3637 C C   . MET   B 1 116 ? -25.610 24.411  -24.237 1.00 40.70  ? 113 MET   B C   1 
ATOM   3638 O O   . MET   B 1 116 ? -25.594 25.355  -25.008 1.00 44.16  ? 113 MET   B O   1 
ATOM   3639 C CB  . MET   B 1 116 ? -27.272 24.785  -22.458 1.00 40.15  ? 113 MET   B CB  1 
ATOM   3640 C CG  . MET   B 1 116 ? -28.182 23.730  -23.050 1.00 44.01  ? 113 MET   B CG  1 
ATOM   3641 S SD  . MET   B 1 116 ? -29.804 23.840  -22.284 1.00 52.87  ? 113 MET   B SD  1 
ATOM   3642 C CE  . MET   B 1 116 ? -30.249 25.513  -22.698 1.00 45.24  ? 113 MET   B CE  1 
ATOM   3643 N N   . VAL   B 1 117 ? -25.441 23.165  -24.629 1.00 36.68  ? 114 VAL   B N   1 
ATOM   3644 C CA  . VAL   B 1 117 ? -25.332 22.832  -26.028 1.00 35.75  ? 114 VAL   B CA  1 
ATOM   3645 C C   . VAL   B 1 117 ? -26.456 21.877  -26.385 1.00 42.21  ? 114 VAL   B C   1 
ATOM   3646 O O   . VAL   B 1 117 ? -26.503 20.759  -25.897 1.00 39.99  ? 114 VAL   B O   1 
ATOM   3647 C CB  . VAL   B 1 117 ? -23.978 22.209  -26.362 1.00 34.84  ? 114 VAL   B CB  1 
ATOM   3648 C CG1 . VAL   B 1 117 ? -23.874 21.954  -27.854 1.00 34.66  ? 114 VAL   B CG1 1 
ATOM   3649 C CG2 . VAL   B 1 117 ? -22.858 23.114  -25.891 1.00 33.45  ? 114 VAL   B CG2 1 
ATOM   3650 N N   . PHE   B 1 118 ? -27.378 22.331  -27.218 1.00 36.38  ? 115 PHE   B N   1 
ATOM   3651 C CA  . PHE   B 1 118 ? -28.481 21.487  -27.639 1.00 40.46  ? 115 PHE   B CA  1 
ATOM   3652 C C   . PHE   B 1 118 ? -27.913 20.324  -28.427 1.00 37.99  ? 115 PHE   B C   1 
ATOM   3653 O O   . PHE   B 1 118 ? -26.985 20.504  -29.191 1.00 33.38  ? 115 PHE   B O   1 
ATOM   3654 C CB  . PHE   B 1 118 ? -29.504 22.286  -28.438 1.00 32.95  ? 115 PHE   B CB  1 
ATOM   3655 C CG  . PHE   B 1 118 ? -30.136 23.402  -27.674 1.00 35.65  ? 115 PHE   B CG  1 
ATOM   3656 C CD1 . PHE   B 1 118 ? -30.910 23.142  -26.565 1.00 35.54  ? 115 PHE   B CD1 1 
ATOM   3657 C CD2 . PHE   B 1 118 ? -29.964 24.709  -28.075 1.00 27.99  ? 115 PHE   B CD2 1 
ATOM   3658 C CE1 . PHE   B 1 118 ? -31.498 24.166  -25.862 1.00 34.73  ? 115 PHE   B CE1 1 
ATOM   3659 C CE2 . PHE   B 1 118 ? -30.550 25.739  -27.378 1.00 32.65  ? 115 PHE   B CE2 1 
ATOM   3660 C CZ  . PHE   B 1 118 ? -31.317 25.468  -26.268 1.00 40.29  ? 115 PHE   B CZ  1 
ATOM   3661 N N   . PRO   B 1 119 ? -28.484 19.123  -28.263 1.00 35.16  ? 116 PRO   B N   1 
ATOM   3662 C CA  . PRO   B 1 119 ? -27.866 17.955  -28.887 1.00 36.98  ? 116 PRO   B CA  1 
ATOM   3663 C C   . PRO   B 1 119 ? -28.051 17.989  -30.392 1.00 38.86  ? 116 PRO   B C   1 
ATOM   3664 O O   . PRO   B 1 119 ? -28.693 18.877  -30.960 1.00 40.56  ? 116 PRO   B O   1 
ATOM   3665 C CB  . PRO   B 1 119 ? -28.601 16.780  -28.257 1.00 31.84  ? 116 PRO   B CB  1 
ATOM   3666 C CG  . PRO   B 1 119 ? -29.923 17.340  -27.905 1.00 38.80  ? 116 PRO   B CG  1 
ATOM   3667 C CD  . PRO   B 1 119 ? -29.670 18.759  -27.476 1.00 36.25  ? 116 PRO   B CD  1 
ATOM   3668 N N   . ALA   B 1 120 ? -27.428 17.022  -31.046 1.00 39.45  ? 117 ALA   B N   1 
ATOM   3669 C CA  . ALA   B 1 120 ? -27.677 16.844  -32.461 1.00 40.87  ? 117 ALA   B CA  1 
ATOM   3670 C C   . ALA   B 1 120 ? -29.016 16.150  -32.625 1.00 37.96  ? 117 ALA   B C   1 
ATOM   3671 O O   . ALA   B 1 120 ? -29.487 15.451  -31.720 1.00 38.68  ? 117 ALA   B O   1 
ATOM   3672 C CB  . ALA   B 1 120 ? -26.558 16.038  -33.127 1.00 33.98  ? 117 ALA   B CB  1 
ATOM   3673 N N   . TYR   B 1 121 ? -29.651 16.385  -33.771 1.00 43.21  ? 118 TYR   B N   1 
ATOM   3674 C CA  . TYR   B 1 121 ? -30.899 15.696  -34.078 1.00 44.55  ? 118 TYR   B CA  1 
ATOM   3675 C C   . TYR   B 1 121 ? -30.653 14.192  -34.111 1.00 44.66  ? 118 TYR   B C   1 
ATOM   3676 O O   . TYR   B 1 121 ? -29.661 13.736  -34.693 1.00 41.17  ? 118 TYR   B O   1 
ATOM   3677 C CB  . TYR   B 1 121 ? -31.451 16.166  -35.424 1.00 36.99  ? 118 TYR   B CB  1 
ATOM   3678 C CG  . TYR   B 1 121 ? -31.861 17.629  -35.529 1.00 41.97  ? 118 TYR   B CG  1 
ATOM   3679 C CD1 . TYR   B 1 121 ? -31.735 18.522  -34.454 1.00 42.29  ? 118 TYR   B CD1 1 
ATOM   3680 C CD2 . TYR   B 1 121 ? -32.396 18.116  -36.716 1.00 43.49  ? 118 TYR   B CD2 1 
ATOM   3681 C CE1 . TYR   B 1 121 ? -32.130 19.863  -34.582 1.00 40.05  ? 118 TYR   B CE1 1 
ATOM   3682 C CE2 . TYR   B 1 121 ? -32.796 19.438  -36.851 1.00 41.21  ? 118 TYR   B CE2 1 
ATOM   3683 C CZ  . TYR   B 1 121 ? -32.665 20.304  -35.793 1.00 44.30  ? 118 TYR   B CZ  1 
ATOM   3684 O OH  . TYR   B 1 121 ? -33.065 21.608  -35.977 1.00 44.64  ? 118 TYR   B OH  1 
ATOM   3685 N N   . ARG   B 1 122 ? -31.538 13.420  -33.467 1.00 36.91  ? 119 ARG   B N   1 
ATOM   3686 C CA  . ARG   B 1 122 ? -31.447 11.963  -33.502 1.00 42.59  ? 119 ARG   B CA  1 
ATOM   3687 C C   . ARG   B 1 122 ? -32.562 11.375  -34.367 1.00 49.25  ? 119 ARG   B C   1 
ATOM   3688 O O   . ARG   B 1 122 ? -33.742 11.715  -34.202 1.00 46.70  ? 119 ARG   B O   1 
ATOM   3689 C CB  . ARG   B 1 122 ? -31.472 11.356  -32.092 1.00 41.03  ? 119 ARG   B CB  1 
ATOM   3690 C CG  . ARG   B 1 122 ? -32.764 11.491  -31.354 1.00 45.82  ? 119 ARG   B CG  1 
ATOM   3691 C CD  . ARG   B 1 122 ? -32.765 10.641  -30.116 1.00 42.67  ? 119 ARG   B CD  1 
ATOM   3692 N NE  . ARG   B 1 122 ? -34.037 10.738  -29.413 1.00 39.80  ? 119 ARG   B NE  1 
ATOM   3693 C CZ  . ARG   B 1 122 ? -34.872 9.726   -29.256 1.00 43.03  ? 119 ARG   B CZ  1 
ATOM   3694 N NH1 . ARG   B 1 122 ? -34.585 8.517   -29.720 1.00 48.03  ? 119 ARG   B NH1 1 
ATOM   3695 N NH2 . ARG   B 1 122 ? -36.012 9.925   -28.597 1.00 43.04  ? 119 ARG   B NH2 1 
ATOM   3696 N N   . LYS   B 1 123 ? -32.180 10.496  -35.292 1.00 46.85  ? 120 LYS   B N   1 
ATOM   3697 C CA  . LYS   B 1 123 ? -33.159 9.845   -36.148 1.00 49.83  ? 120 LYS   B CA  1 
ATOM   3698 C C   . LYS   B 1 123 ? -34.092 8.973   -35.327 1.00 52.36  ? 120 LYS   B C   1 
ATOM   3699 O O   . LYS   B 1 123 ? -33.675 8.283   -34.398 1.00 53.66  ? 120 LYS   B O   1 
ATOM   3700 C CB  . LYS   B 1 123 ? -32.468 8.996   -37.216 1.00 53.71  ? 120 LYS   B CB  1 
ATOM   3701 C CG  . LYS   B 1 123 ? -33.390 7.964   -37.855 1.00 57.65  ? 120 LYS   B CG  1 
ATOM   3702 C CD  . LYS   B 1 123 ? -32.735 7.208   -39.001 1.00 58.83  ? 120 LYS   B CD  1 
ATOM   3703 C CE  . LYS   B 1 123 ? -32.519 8.113   -40.195 1.00 58.70  ? 120 LYS   B CE  1 
ATOM   3704 N NZ  . LYS   B 1 123 ? -32.064 7.339   -41.384 1.00 61.59  ? 120 LYS   B NZ  1 
ATOM   3705 N N   . LEU   B 1 124 ? -35.369 9.031   -35.654 1.00 55.89  ? 121 LEU   B N   1 
ATOM   3706 C CA  . LEU   B 1 124 ? -36.319 8.044   -35.186 1.00 55.44  ? 121 LEU   B CA  1 
ATOM   3707 C C   . LEU   B 1 124 ? -36.579 7.073   -36.324 1.00 59.93  ? 121 LEU   B C   1 
ATOM   3708 O O   . LEU   B 1 124 ? -36.388 7.406   -37.494 1.00 65.89  ? 121 LEU   B O   1 
ATOM   3709 C CB  . LEU   B 1 124 ? -37.612 8.714   -34.743 1.00 55.12  ? 121 LEU   B CB  1 
ATOM   3710 C CG  . LEU   B 1 124 ? -37.422 9.872   -33.774 1.00 49.39  ? 121 LEU   B CG  1 
ATOM   3711 C CD1 . LEU   B 1 124 ? -38.737 10.625  -33.622 1.00 46.10  ? 121 LEU   B CD1 1 
ATOM   3712 C CD2 . LEU   B 1 124 ? -36.955 9.324   -32.437 1.00 46.46  ? 121 LEU   B CD2 1 
ATOM   3713 N N   . ASP   B 1 125 ? -36.995 5.857   -35.981 1.00 67.49  ? 122 ASP   B N   1 
ATOM   3714 C CA  . ASP   B 1 125 ? -37.378 4.891   -37.005 1.00 72.87  ? 122 ASP   B CA  1 
ATOM   3715 C C   . ASP   B 1 125 ? -38.694 4.242   -36.609 1.00 69.42  ? 122 ASP   B C   1 
ATOM   3716 O O   . ASP   B 1 125 ? -38.865 3.829   -35.459 1.00 67.43  ? 122 ASP   B O   1 
ATOM   3717 C CB  . ASP   B 1 125 ? -36.278 3.844   -37.231 1.00 81.59  ? 122 ASP   B CB  1 
ATOM   3718 C CG  . ASP   B 1 125 ? -36.791 2.579   -37.914 1.00 90.87  ? 122 ASP   B CG  1 
ATOM   3719 O OD1 . ASP   B 1 125 ? -36.910 2.551   -39.168 1.00 88.02  ? 122 ASP   B OD1 1 
ATOM   3720 O OD2 . ASP   B 1 125 ? -37.060 1.605   -37.173 1.00 90.92  ? 122 ASP   B OD2 1 
ATOM   3721 N N   . LEU   B 1 126 ? -39.609 4.146   -37.579 1.00 68.71  ? 123 LEU   B N   1 
ATOM   3722 C CA  . LEU   B 1 126 ? -41.020 3.896   -37.286 1.00 69.82  ? 123 LEU   B CA  1 
ATOM   3723 C C   . LEU   B 1 126 ? -41.257 2.523   -36.682 1.00 72.51  ? 123 LEU   B C   1 
ATOM   3724 O O   . LEU   B 1 126 ? -42.229 2.337   -35.934 1.00 69.43  ? 123 LEU   B O   1 
ATOM   3725 C CB  . LEU   B 1 126 ? -41.852 4.051   -38.558 1.00 70.26  ? 123 LEU   B CB  1 
ATOM   3726 C CG  . LEU   B 1 126 ? -42.589 5.377   -38.629 1.00 65.34  ? 123 LEU   B CG  1 
ATOM   3727 C CD1 . LEU   B 1 126 ? -43.578 5.457   -37.477 1.00 61.01  ? 123 LEU   B CD1 1 
ATOM   3728 C CD2 . LEU   B 1 126 ? -41.580 6.494   -38.545 1.00 65.57  ? 123 LEU   B CD2 1 
ATOM   3729 N N   . ARG   B 1 127 ? -40.389 1.558   -36.994 1.00 76.18  ? 124 ARG   B N   1 
ATOM   3730 C CA  . ARG   B 1 127 ? -40.611 0.182   -36.564 1.00 75.77  ? 124 ARG   B CA  1 
ATOM   3731 C C   . ARG   B 1 127 ? -40.753 0.082   -35.045 1.00 78.35  ? 124 ARG   B C   1 
ATOM   3732 O O   . ARG   B 1 127 ? -41.612 -0.657  -34.543 1.00 78.35  ? 124 ARG   B O   1 
ATOM   3733 C CB  . ARG   B 1 127 ? -39.473 -0.693  -37.085 1.00 83.73  ? 124 ARG   B CB  1 
ATOM   3734 C CG  . ARG   B 1 127 ? -39.165 -0.439  -38.575 1.00 87.73  ? 124 ARG   B CG  1 
ATOM   3735 C CD  . ARG   B 1 127 ? -37.911 -1.179  -39.042 1.00 94.12  ? 124 ARG   B CD  1 
ATOM   3736 N NE  . ARG   B 1 127 ? -36.803 -1.019  -38.104 1.00 98.40  ? 124 ARG   B NE  1 
ATOM   3737 C CZ  . ARG   B 1 127 ? -35.535 -1.304  -38.376 1.00 98.28  ? 124 ARG   B CZ  1 
ATOM   3738 N NH1 . ARG   B 1 127 ? -35.170 -1.761  -39.564 1.00 90.73  ? 124 ARG   B NH1 1 
ATOM   3739 N NH2 . ARG   B 1 127 ? -34.610 -1.117  -37.435 1.00 94.93  ? 124 ARG   B NH2 1 
ATOM   3740 N N   . HIS   B 1 128 ? -39.960 0.853   -34.295 1.00 75.15  ? 125 HIS   B N   1 
ATOM   3741 C CA  . HIS   B 1 128 ? -40.058 0.805   -32.838 1.00 71.58  ? 125 HIS   B CA  1 
ATOM   3742 C C   . HIS   B 1 128 ? -41.370 1.370   -32.305 1.00 69.02  ? 125 HIS   B C   1 
ATOM   3743 O O   . HIS   B 1 128 ? -41.589 1.343   -31.089 1.00 69.67  ? 125 HIS   B O   1 
ATOM   3744 C CB  . HIS   B 1 128 ? -38.882 1.555   -32.205 1.00 68.50  ? 125 HIS   B CB  1 
ATOM   3745 C CG  . HIS   B 1 128 ? -37.648 1.553   -33.046 1.00 77.88  ? 125 HIS   B CG  1 
ATOM   3746 N ND1 . HIS   B 1 128 ? -37.253 2.649   -33.782 1.00 81.80  ? 125 HIS   B ND1 1 
ATOM   3747 C CD2 . HIS   B 1 128 ? -36.730 0.584   -33.292 1.00 85.03  ? 125 HIS   B CD2 1 
ATOM   3748 C CE1 . HIS   B 1 128 ? -36.131 2.363   -34.426 1.00 83.21  ? 125 HIS   B CE1 1 
ATOM   3749 N NE2 . HIS   B 1 128 ? -35.797 1.112   -34.157 1.00 84.27  ? 125 HIS   B NE2 1 
ATOM   3750 N N   . TYR   B 1 129 ? -42.252 1.867   -33.163 1.00 65.28  ? 126 TYR   B N   1 
ATOM   3751 C CA  . TYR   B 1 129 ? -43.466 2.518   -32.704 1.00 63.04  ? 126 TYR   B CA  1 
ATOM   3752 C C   . TYR   B 1 129 ? -44.691 1.789   -33.232 1.00 66.93  ? 126 TYR   B C   1 
ATOM   3753 O O   . TYR   B 1 129 ? -44.660 1.130   -34.276 1.00 68.71  ? 126 TYR   B O   1 
ATOM   3754 C CB  . TYR   B 1 129 ? -43.494 3.990   -33.129 1.00 64.05  ? 126 TYR   B CB  1 
ATOM   3755 C CG  . TYR   B 1 129 ? -42.247 4.731   -32.706 1.00 66.44  ? 126 TYR   B CG  1 
ATOM   3756 C CD1 . TYR   B 1 129 ? -41.135 4.790   -33.542 1.00 63.86  ? 126 TYR   B CD1 1 
ATOM   3757 C CD2 . TYR   B 1 129 ? -42.167 5.340   -31.458 1.00 61.59  ? 126 TYR   B CD2 1 
ATOM   3758 C CE1 . TYR   B 1 129 ? -39.989 5.446   -33.157 1.00 63.45  ? 126 TYR   B CE1 1 
ATOM   3759 C CE2 . TYR   B 1 129 ? -41.021 6.001   -31.063 1.00 60.02  ? 126 TYR   B CE2 1 
ATOM   3760 C CZ  . TYR   B 1 129 ? -39.935 6.049   -31.917 1.00 57.83  ? 126 TYR   B CZ  1 
ATOM   3761 O OH  . TYR   B 1 129 ? -38.790 6.704   -31.536 1.00 53.83  ? 126 TYR   B OH  1 
ATOM   3762 N N   . ASP   B 1 130 ? -45.775 1.931   -32.483 1.00 62.35  ? 127 ASP   B N   1 
ATOM   3763 C CA  . ASP   B 1 130 ? -47.046 1.289   -32.753 1.00 66.44  ? 127 ASP   B CA  1 
ATOM   3764 C C   . ASP   B 1 130 ? -48.099 2.073   -31.967 1.00 68.77  ? 127 ASP   B C   1 
ATOM   3765 O O   . ASP   B 1 130 ? -47.837 3.192   -31.514 1.00 66.21  ? 127 ASP   B O   1 
ATOM   3766 C CB  . ASP   B 1 130 ? -46.968 -0.203  -32.398 1.00 71.46  ? 127 ASP   B CB  1 
ATOM   3767 C CG  . ASP   B 1 130 ? -46.502 -0.443  -30.960 1.00 79.07  ? 127 ASP   B CG  1 
ATOM   3768 O OD1 . ASP   B 1 130 ? -47.266 -0.081  -30.042 1.00 78.66  ? 127 ASP   B OD1 1 
ATOM   3769 O OD2 . ASP   B 1 130 ? -45.386 -0.984  -30.741 1.00 76.21  ? 127 ASP   B OD2 1 
ATOM   3770 N N   . ASP   B 1 131 ? -49.279 1.493   -31.787 1.00 70.10  ? 128 ASP   B N   1 
ATOM   3771 C CA  . ASP   B 1 131 ? -50.320 2.189   -31.042 1.00 71.31  ? 128 ASP   B CA  1 
ATOM   3772 C C   . ASP   B 1 131 ? -50.081 2.167   -29.532 1.00 72.97  ? 128 ASP   B C   1 
ATOM   3773 O O   . ASP   B 1 131 ? -50.749 2.905   -28.797 1.00 70.77  ? 128 ASP   B O   1 
ATOM   3774 C CB  . ASP   B 1 131 ? -51.684 1.578   -31.389 1.00 77.93  ? 128 ASP   B CB  1 
ATOM   3775 C CG  . ASP   B 1 131 ? -52.785 2.623   -31.516 1.00 76.35  ? 128 ASP   B CG  1 
ATOM   3776 O OD1 . ASP   B 1 131 ? -53.250 3.127   -30.474 1.00 80.80  ? 128 ASP   B OD1 1 
ATOM   3777 O OD2 . ASP   B 1 131 ? -53.182 2.942   -32.659 1.00 78.26  ? 128 ASP   B OD2 1 
ATOM   3778 N N   . ALA   B 1 132 ? -49.147 1.346   -29.050 1.00 71.54  ? 129 ALA   B N   1 
ATOM   3779 C CA  . ALA   B 1 132 ? -48.813 1.344   -27.630 1.00 74.37  ? 129 ALA   B CA  1 
ATOM   3780 C C   . ALA   B 1 132 ? -47.645 2.276   -27.335 1.00 73.10  ? 129 ALA   B C   1 
ATOM   3781 O O   . ALA   B 1 132 ? -47.633 2.958   -26.302 1.00 69.69  ? 129 ALA   B O   1 
ATOM   3782 C CB  . ALA   B 1 132 ? -48.498 -0.080  -27.160 1.00 74.54  ? 129 ALA   B CB  1 
ATOM   3783 N N   . LEU   B 1 133 ? -46.672 2.328   -28.235 1.00 68.56  ? 130 LEU   B N   1 
ATOM   3784 C CA  . LEU   B 1 133 ? -45.670 3.375   -28.182 1.00 63.01  ? 130 LEU   B CA  1 
ATOM   3785 C C   . LEU   B 1 133 ? -45.795 4.259   -29.412 1.00 57.12  ? 130 LEU   B C   1 
ATOM   3786 O O   . LEU   B 1 133 ? -44.995 4.115   -30.346 1.00 57.66  ? 130 LEU   B O   1 
ATOM   3787 C CB  . LEU   B 1 133 ? -44.269 2.785   -28.103 1.00 66.26  ? 130 LEU   B CB  1 
ATOM   3788 C CG  . LEU   B 1 133 ? -43.810 2.567   -26.670 1.00 67.19  ? 130 LEU   B CG  1 
ATOM   3789 C CD1 . LEU   B 1 133 ? -42.304 2.397   -26.650 1.00 66.16  ? 130 LEU   B CD1 1 
ATOM   3790 C CD2 . LEU   B 1 133 ? -44.256 3.719   -25.786 1.00 57.50  ? 130 LEU   B CD2 1 
ATOM   3791 N N   . PRO   B 1 134 ? -46.774 5.171   -29.452 1.00 51.02  ? 131 PRO   B N   1 
ATOM   3792 C CA  . PRO   B 1 134 ? -46.926 6.037   -30.629 1.00 50.99  ? 131 PRO   B CA  1 
ATOM   3793 C C   . PRO   B 1 134 ? -45.680 6.876   -30.880 1.00 52.83  ? 131 PRO   B C   1 
ATOM   3794 O O   . PRO   B 1 134 ? -44.874 7.120   -29.978 1.00 52.46  ? 131 PRO   B O   1 
ATOM   3795 C CB  . PRO   B 1 134 ? -48.142 6.908   -30.282 1.00 44.98  ? 131 PRO   B CB  1 
ATOM   3796 C CG  . PRO   B 1 134 ? -48.309 6.803   -28.808 1.00 56.54  ? 131 PRO   B CG  1 
ATOM   3797 C CD  . PRO   B 1 134 ? -47.796 5.445   -28.427 1.00 58.44  ? 131 PRO   B CD  1 
ATOM   3798 N N   . LEU   B 1 135 ? -45.512 7.286   -32.142 1.00 49.30  ? 132 LEU   B N   1 
ATOM   3799 C CA  . LEU   B 1 135 ? -44.356 8.087   -32.529 1.00 47.77  ? 132 LEU   B CA  1 
ATOM   3800 C C   . LEU   B 1 135 ? -44.154 9.277   -31.606 1.00 49.74  ? 132 LEU   B C   1 
ATOM   3801 O O   . LEU   B 1 135 ? -43.016 9.697   -31.374 1.00 50.36  ? 132 LEU   B O   1 
ATOM   3802 C CB  . LEU   B 1 135 ? -44.516 8.579   -33.964 1.00 51.95  ? 132 LEU   B CB  1 
ATOM   3803 C CG  . LEU   B 1 135 ? -43.428 9.541   -34.445 1.00 50.94  ? 132 LEU   B CG  1 
ATOM   3804 C CD1 . LEU   B 1 135 ? -42.125 8.791   -34.698 1.00 47.56  ? 132 LEU   B CD1 1 
ATOM   3805 C CD2 . LEU   B 1 135 ? -43.890 10.301  -35.678 1.00 43.17  ? 132 LEU   B CD2 1 
ATOM   3806 N N   . SER   B 1 136 ? -45.239 9.809   -31.043 1.00 44.90  ? 133 SER   B N   1 
ATOM   3807 C CA  . SER   B 1 136 ? -45.145 10.971  -30.181 1.00 41.37  ? 133 SER   B CA  1 
ATOM   3808 C C   . SER   B 1 136 ? -44.411 10.693  -28.872 1.00 52.45  ? 133 SER   B C   1 
ATOM   3809 O O   . SER   B 1 136 ? -44.159 11.642  -28.116 1.00 48.05  ? 133 SER   B O   1 
ATOM   3810 C CB  . SER   B 1 136 ? -46.546 11.500  -29.877 1.00 45.12  ? 133 SER   B CB  1 
ATOM   3811 O OG  . SER   B 1 136 ? -47.114 10.808  -28.787 1.00 44.67  ? 133 SER   B OG  1 
ATOM   3812 N N   . THR   B 1 137 ? -44.090 9.427   -28.568 1.00 51.62  ? 134 THR   B N   1 
ATOM   3813 C CA  . THR   B 1 137 ? -43.384 9.125   -27.330 1.00 46.53  ? 134 THR   B CA  1 
ATOM   3814 C C   . THR   B 1 137 ? -41.930 9.560   -27.395 1.00 46.52  ? 134 THR   B C   1 
ATOM   3815 O O   . THR   B 1 137 ? -41.295 9.692   -26.342 1.00 45.90  ? 134 THR   B O   1 
ATOM   3816 C CB  . THR   B 1 137 ? -43.469 7.630   -26.984 1.00 47.06  ? 134 THR   B CB  1 
ATOM   3817 O OG1 . THR   B 1 137 ? -43.138 6.831   -28.127 1.00 49.83  ? 134 THR   B OG1 1 
ATOM   3818 C CG2 . THR   B 1 137 ? -44.862 7.279   -26.510 1.00 50.14  ? 134 THR   B CG2 1 
ATOM   3819 N N   . ALA   B 1 138 ? -41.403 9.824   -28.601 1.00 45.04  ? 135 ALA   B N   1 
ATOM   3820 C CA  . ALA   B 1 138 ? -40.065 10.401  -28.735 1.00 49.49  ? 135 ALA   B CA  1 
ATOM   3821 C C   . ALA   B 1 138 ? -39.954 11.803  -28.119 1.00 49.46  ? 135 ALA   B C   1 
ATOM   3822 O O   . ALA   B 1 138 ? -38.841 12.349  -28.056 1.00 51.43  ? 135 ALA   B O   1 
ATOM   3823 C CB  . ALA   B 1 138 ? -39.641 10.436  -30.206 1.00 37.69  ? 135 ALA   B CB  1 
ATOM   3824 N N   . LEU   B 1 139 ? -41.072 12.395  -27.680 1.00 42.00  ? 136 LEU   B N   1 
ATOM   3825 C CA  . LEU   B 1 139 ? -41.078 13.616  -26.885 1.00 41.55  ? 136 LEU   B CA  1 
ATOM   3826 C C   . LEU   B 1 139 ? -41.467 13.365  -25.440 1.00 45.28  ? 136 LEU   B C   1 
ATOM   3827 O O   . LEU   B 1 139 ? -41.550 14.323  -24.662 1.00 48.95  ? 136 LEU   B O   1 
ATOM   3828 C CB  . LEU   B 1 139 ? -42.027 14.655  -27.491 1.00 42.11  ? 136 LEU   B CB  1 
ATOM   3829 C CG  . LEU   B 1 139 ? -41.526 15.147  -28.848 1.00 44.47  ? 136 LEU   B CG  1 
ATOM   3830 C CD1 . LEU   B 1 139 ? -42.515 16.107  -29.518 1.00 37.46  ? 136 LEU   B CD1 1 
ATOM   3831 C CD2 . LEU   B 1 139 ? -40.173 15.795  -28.673 1.00 39.38  ? 136 LEU   B CD2 1 
ATOM   3832 N N   . GLY   B 1 140 ? -41.712 12.111  -25.059 1.00 45.12  ? 137 GLY   B N   1 
ATOM   3833 C CA  . GLY   B 1 140 ? -42.038 11.783  -23.683 1.00 51.95  ? 137 GLY   B CA  1 
ATOM   3834 C C   . GLY   B 1 140 ? -41.312 10.557  -23.161 1.00 53.17  ? 137 GLY   B C   1 
ATOM   3835 O O   . GLY   B 1 140 ? -40.081 10.585  -23.018 1.00 49.06  ? 137 GLY   B O   1 
ATOM   3836 N N   . VAL   B 1 141 ? -42.053 9.469   -22.899 1.00 52.47  ? 138 VAL   B N   1 
ATOM   3837 C CA  . VAL   B 1 141 ? -41.449 8.282   -22.294 1.00 48.94  ? 138 VAL   B CA  1 
ATOM   3838 C C   . VAL   B 1 141 ? -40.251 7.809   -23.109 1.00 47.54  ? 138 VAL   B C   1 
ATOM   3839 O O   . VAL   B 1 141 ? -39.246 7.361   -22.546 1.00 53.37  ? 138 VAL   B O   1 
ATOM   3840 C CB  . VAL   B 1 141 ? -42.493 7.156   -22.103 1.00 52.94  ? 138 VAL   B CB  1 
ATOM   3841 C CG1 . VAL   B 1 141 ? -42.997 6.602   -23.445 1.00 47.92  ? 138 VAL   B CG1 1 
ATOM   3842 C CG2 . VAL   B 1 141 ? -41.880 6.043   -21.276 1.00 48.63  ? 138 VAL   B CG2 1 
ATOM   3843 N N   . MET   B 1 142 ? -40.319 7.917   -24.438 1.00 42.40  ? 139 MET   B N   1 
ATOM   3844 C CA  . MET   B 1 142 ? -39.185 7.573   -25.291 1.00 44.17  ? 139 MET   B CA  1 
ATOM   3845 C C   . MET   B 1 142 ? -38.394 8.801   -25.720 1.00 44.13  ? 139 MET   B C   1 
ATOM   3846 O O   . MET   B 1 142 ? -37.656 8.748   -26.711 1.00 44.23  ? 139 MET   B O   1 
ATOM   3847 C CB  . MET   B 1 142 ? -39.636 6.794   -26.530 1.00 48.24  ? 139 MET   B CB  1 
ATOM   3848 C CG  . MET   B 1 142 ? -40.303 5.461   -26.234 1.00 52.32  ? 139 MET   B CG  1 
ATOM   3849 S SD  . MET   B 1 142 ? -39.225 4.288   -25.392 1.00 61.08  ? 139 MET   B SD  1 
ATOM   3850 C CE  . MET   B 1 142 ? -39.970 4.334   -23.755 1.00 48.71  ? 139 MET   B CE  1 
ATOM   3851 N N   . GLY   B 1 143 ? -38.542 9.908   -25.007 1.00 44.42  ? 140 GLY   B N   1 
ATOM   3852 C CA  . GLY   B 1 143 ? -37.794 11.106  -25.306 1.00 46.01  ? 140 GLY   B CA  1 
ATOM   3853 C C   . GLY   B 1 143 ? -37.151 11.676  -24.057 1.00 44.97  ? 140 GLY   B C   1 
ATOM   3854 O O   . GLY   B 1 143 ? -36.824 10.961  -23.111 1.00 47.88  ? 140 GLY   B O   1 
ATOM   3855 N N   . GLY   B 1 144 ? -36.993 12.994  -24.071 1.00 46.56  ? 141 GLY   B N   1 
ATOM   3856 C CA  . GLY   B 1 144 ? -36.386 13.721  -22.989 1.00 37.31  ? 141 GLY   B CA  1 
ATOM   3857 C C   . GLY   B 1 144 ? -36.861 13.319  -21.610 1.00 38.29  ? 141 GLY   B C   1 
ATOM   3858 O O   . GLY   B 1 144 ? -36.063 12.914  -20.766 1.00 41.60  ? 141 GLY   B O   1 
ATOM   3859 N N   . PRO   B 1 145 ? -38.161 13.452  -21.333 1.00 43.58  ? 142 PRO   B N   1 
ATOM   3860 C CA  . PRO   B 1 145 ? -38.612 13.220  -19.950 1.00 41.02  ? 142 PRO   B CA  1 
ATOM   3861 C C   . PRO   B 1 145 ? -38.422 11.778  -19.501 1.00 45.77  ? 142 PRO   B C   1 
ATOM   3862 O O   . PRO   B 1 145 ? -38.040 11.531  -18.347 1.00 45.29  ? 142 PRO   B O   1 
ATOM   3863 C CB  . PRO   B 1 145 ? -40.090 13.642  -19.981 1.00 42.34  ? 142 PRO   B CB  1 
ATOM   3864 C CG  . PRO   B 1 145 ? -40.229 14.494  -21.234 1.00 45.76  ? 142 PRO   B CG  1 
ATOM   3865 C CD  . PRO   B 1 145 ? -39.257 13.913  -22.208 1.00 42.45  ? 142 PRO   B CD  1 
ATOM   3866 N N   . GLY   B 1 146 ? -38.645 10.812  -20.390 1.00 43.21  ? 143 GLY   B N   1 
ATOM   3867 C CA  . GLY   B 1 146 ? -38.335 9.437   -20.045 1.00 44.15  ? 143 GLY   B CA  1 
ATOM   3868 C C   . GLY   B 1 146 ? -36.862 9.233   -19.744 1.00 42.37  ? 143 GLY   B C   1 
ATOM   3869 O O   . GLY   B 1 146 ? -36.503 8.487   -18.832 1.00 39.74  ? 143 GLY   B O   1 
ATOM   3870 N N   . MET   B 1 147 ? -35.986 9.893   -20.509 1.00 46.38  ? 144 MET   B N   1 
ATOM   3871 C CA  . MET   B 1 147 ? -34.552 9.767   -20.253 1.00 42.59  ? 144 MET   B CA  1 
ATOM   3872 C C   . MET   B 1 147 ? -34.180 10.386  -18.919 1.00 43.92  ? 144 MET   B C   1 
ATOM   3873 O O   . MET   B 1 147 ? -33.236 9.928   -18.264 1.00 46.88  ? 144 MET   B O   1 
ATOM   3874 C CB  . MET   B 1 147 ? -33.748 10.408  -21.382 1.00 41.52  ? 144 MET   B CB  1 
ATOM   3875 C CG  . MET   B 1 147 ? -32.246 10.293  -21.207 1.00 42.33  ? 144 MET   B CG  1 
ATOM   3876 S SD  . MET   B 1 147 ? -31.714 8.594   -21.230 1.00 44.36  ? 144 MET   B SD  1 
ATOM   3877 C CE  . MET   B 1 147 ? -31.546 8.264   -22.984 1.00 42.47  ? 144 MET   B CE  1 
ATOM   3878 N N   . THR   B 1 148 ? -34.933 11.400  -18.493 1.00 40.32  ? 145 THR   B N   1 
ATOM   3879 C CA  . THR   B 1 148 ? -34.677 12.048  -17.217 1.00 40.92  ? 145 THR   B CA  1 
ATOM   3880 C C   . THR   B 1 148 ? -35.023 11.122  -16.056 1.00 42.82  ? 145 THR   B C   1 
ATOM   3881 O O   . THR   B 1 148 ? -34.232 10.966  -15.119 1.00 42.23  ? 145 THR   B O   1 
ATOM   3882 C CB  . THR   B 1 148 ? -35.470 13.356  -17.153 1.00 39.78  ? 145 THR   B CB  1 
ATOM   3883 O OG1 . THR   B 1 148 ? -35.082 14.184  -18.259 1.00 44.63  ? 145 THR   B OG1 1 
ATOM   3884 C CG2 . THR   B 1 148 ? -35.219 14.101  -15.849 1.00 35.07  ? 145 THR   B CG2 1 
ATOM   3885 N N   . ALA   B 1 149 ? -36.186 10.472  -16.115 1.00 42.24  ? 146 ALA   B N   1 
ATOM   3886 C CA  . ALA   B 1 149 ? -36.602 9.603   -15.015 1.00 46.28  ? 146 ALA   B CA  1 
ATOM   3887 C C   . ALA   B 1 149 ? -35.783 8.311   -14.981 1.00 42.76  ? 146 ALA   B C   1 
ATOM   3888 O O   . ALA   B 1 149 ? -35.168 7.979   -13.959 1.00 43.90  ? 146 ALA   B O   1 
ATOM   3889 C CB  . ALA   B 1 149 ? -38.100 9.301   -15.120 1.00 44.50  ? 146 ALA   B CB  1 
ATOM   3890 N N   . TRP   B 1 150 ? -35.762 7.571   -16.091 1.00 39.44  ? 147 TRP   B N   1 
ATOM   3891 C CA  . TRP   B 1 150 ? -35.038 6.302   -16.138 1.00 44.66  ? 147 TRP   B CA  1 
ATOM   3892 C C   . TRP   B 1 150 ? -33.551 6.486   -15.835 1.00 46.50  ? 147 TRP   B C   1 
ATOM   3893 O O   . TRP   B 1 150 ? -32.925 5.636   -15.186 1.00 44.71  ? 147 TRP   B O   1 
ATOM   3894 C CB  . TRP   B 1 150 ? -35.225 5.651   -17.509 1.00 40.07  ? 147 TRP   B CB  1 
ATOM   3895 C CG  . TRP   B 1 150 ? -34.309 4.505   -17.765 1.00 41.56  ? 147 TRP   B CG  1 
ATOM   3896 C CD1 . TRP   B 1 150 ? -34.468 3.226   -17.337 1.00 44.82  ? 147 TRP   B CD1 1 
ATOM   3897 C CD2 . TRP   B 1 150 ? -33.084 4.528   -18.518 1.00 43.02  ? 147 TRP   B CD2 1 
ATOM   3898 N NE1 . TRP   B 1 150 ? -33.424 2.444   -17.774 1.00 49.31  ? 147 TRP   B NE1 1 
ATOM   3899 C CE2 . TRP   B 1 150 ? -32.559 3.221   -18.499 1.00 45.14  ? 147 TRP   B CE2 1 
ATOM   3900 C CE3 . TRP   B 1 150 ? -32.379 5.526   -19.197 1.00 42.22  ? 147 TRP   B CE3 1 
ATOM   3901 C CZ2 . TRP   B 1 150 ? -31.360 2.882   -19.133 1.00 46.85  ? 147 TRP   B CZ2 1 
ATOM   3902 C CZ3 . TRP   B 1 150 ? -31.185 5.192   -19.826 1.00 48.47  ? 147 TRP   B CZ3 1 
ATOM   3903 C CH2 . TRP   B 1 150 ? -30.688 3.876   -19.792 1.00 48.40  ? 147 TRP   B CH2 1 
ATOM   3904 N N   . GLY   B 1 151 ? -32.969 7.592   -16.293 1.00 43.84  ? 148 GLY   B N   1 
ATOM   3905 C CA  . GLY   B 1 151 ? -31.562 7.829   -16.035 1.00 37.11  ? 148 GLY   B CA  1 
ATOM   3906 C C   . GLY   B 1 151 ? -31.276 8.137   -14.577 1.00 39.97  ? 148 GLY   B C   1 
ATOM   3907 O O   . GLY   B 1 151 ? -30.240 7.733   -14.049 1.00 45.45  ? 148 GLY   B O   1 
ATOM   3908 N N   . THR   B 1 152 ? -32.175 8.866   -13.906 1.00 36.71  ? 149 THR   B N   1 
ATOM   3909 C CA  . THR   B 1 152 ? -32.004 9.076   -12.472 1.00 40.25  ? 149 THR   B CA  1 
ATOM   3910 C C   . THR   B 1 152 ? -32.140 7.766   -11.706 1.00 44.47  ? 149 THR   B C   1 
ATOM   3911 O O   . THR   B 1 152 ? -31.397 7.523   -10.747 1.00 43.42  ? 149 THR   B O   1 
ATOM   3912 C CB  . THR   B 1 152 ? -33.012 10.105  -11.954 1.00 40.52  ? 149 THR   B CB  1 
ATOM   3913 O OG1 . THR   B 1 152 ? -32.660 11.392  -12.460 1.00 43.04  ? 149 THR   B OG1 1 
ATOM   3914 C CG2 . THR   B 1 152 ? -33.048 10.157  -10.392 1.00 33.04  ? 149 THR   B CG2 1 
ATOM   3915 N N   . MET   B 1 153 ? -33.075 6.906   -12.119 1.00 42.31  ? 150 MET   B N   1 
ATOM   3916 C CA  . MET   B 1 153 ? -33.344 5.696   -11.360 1.00 42.22  ? 150 MET   B CA  1 
ATOM   3917 C C   . MET   B 1 153 ? -32.352 4.581   -11.640 1.00 42.93  ? 150 MET   B C   1 
ATOM   3918 O O   . MET   B 1 153 ? -32.185 3.702   -10.792 1.00 55.95  ? 150 MET   B O   1 
ATOM   3919 C CB  . MET   B 1 153 ? -34.755 5.190   -11.644 1.00 41.04  ? 150 MET   B CB  1 
ATOM   3920 C CG  . MET   B 1 153 ? -35.834 6.146   -11.254 1.00 39.59  ? 150 MET   B CG  1 
ATOM   3921 S SD  . MET   B 1 153 ? -35.410 7.109   -9.819  1.00 52.81  ? 150 MET   B SD  1 
ATOM   3922 C CE  . MET   B 1 153 ? -36.496 6.420   -8.578  1.00 41.93  ? 150 MET   B CE  1 
ATOM   3923 N N   . THR   B 1 154 ? -31.708 4.570   -12.795 1.00 35.28  ? 151 THR   B N   1 
ATOM   3924 C CA  . THR   B 1 154 ? -30.756 3.517   -13.081 1.00 41.27  ? 151 THR   B CA  1 
ATOM   3925 C C   . THR   B 1 154 ? -29.317 3.981   -13.008 1.00 45.48  ? 151 THR   B C   1 
ATOM   3926 O O   . THR   B 1 154 ? -28.420 3.132   -13.008 1.00 45.09  ? 151 THR   B O   1 
ATOM   3927 C CB  . THR   B 1 154 ? -31.009 2.903   -14.465 1.00 42.52  ? 151 THR   B CB  1 
ATOM   3928 O OG1 . THR   B 1 154 ? -30.883 3.908   -15.472 1.00 40.16  ? 151 THR   B OG1 1 
ATOM   3929 C CG2 . THR   B 1 154 ? -32.391 2.314   -14.529 1.00 45.17  ? 151 THR   B CG2 1 
ATOM   3930 N N   . LYS   B 1 155 ? -29.067 5.295   -12.945 1.00 43.56  ? 152 LYS   B N   1 
ATOM   3931 C CA  . LYS   B 1 155 ? -27.708 5.809   -12.896 1.00 39.32  ? 152 LYS   B CA  1 
ATOM   3932 C C   . LYS   B 1 155 ? -27.369 6.601   -11.637 1.00 41.94  ? 152 LYS   B C   1 
ATOM   3933 O O   . LYS   B 1 155 ? -26.181 6.875   -11.419 1.00 44.19  ? 152 LYS   B O   1 
ATOM   3934 C CB  . LYS   B 1 155 ? -27.412 6.705   -14.103 1.00 36.47  ? 152 LYS   B CB  1 
ATOM   3935 C CG  . LYS   B 1 155 ? -27.733 6.143   -15.454 1.00 46.12  ? 152 LYS   B CG  1 
ATOM   3936 C CD  . LYS   B 1 155 ? -27.165 7.079   -16.537 1.00 42.42  ? 152 LYS   B CD  1 
ATOM   3937 C CE  . LYS   B 1 155 ? -27.645 6.667   -17.897 1.00 42.83  ? 152 LYS   B CE  1 
ATOM   3938 N NZ  . LYS   B 1 155 ? -27.344 5.231   -18.175 1.00 47.22  ? 152 LYS   B NZ  1 
ATOM   3939 N N   . PHE   B 1 156 ? -28.352 7.000   -10.820 1.00 36.04  ? 153 PHE   B N   1 
ATOM   3940 C CA  . PHE   B 1 156 ? -28.041 7.718   -9.582  1.00 35.96  ? 153 PHE   B CA  1 
ATOM   3941 C C   . PHE   B 1 156 ? -28.710 7.087   -8.372  1.00 36.15  ? 153 PHE   B C   1 
ATOM   3942 O O   . PHE   B 1 156 ? -28.028 6.565   -7.480  1.00 41.36  ? 153 PHE   B O   1 
ATOM   3943 C CB  . PHE   B 1 156 ? -28.453 9.193   -9.657  1.00 35.51  ? 153 PHE   B CB  1 
ATOM   3944 C CG  . PHE   B 1 156 ? -28.396 9.918   -8.321  1.00 35.00  ? 153 PHE   B CG  1 
ATOM   3945 C CD1 . PHE   B 1 156 ? -27.222 9.942   -7.570  1.00 33.53  ? 153 PHE   B CD1 1 
ATOM   3946 C CD2 . PHE   B 1 156 ? -29.505 10.586  -7.829  1.00 31.24  ? 153 PHE   B CD2 1 
ATOM   3947 C CE1 . PHE   B 1 156 ? -27.159 10.603  -6.342  1.00 28.68  ? 153 PHE   B CE1 1 
ATOM   3948 C CE2 . PHE   B 1 156 ? -29.448 11.256  -6.613  1.00 36.11  ? 153 PHE   B CE2 1 
ATOM   3949 C CZ  . PHE   B 1 156 ? -28.264 11.263  -5.867  1.00 32.97  ? 153 PHE   B CZ  1 
ATOM   3950 N N   . MET   B 1 157 ? -30.033 7.174   -8.302  1.00 37.81  ? 154 MET   B N   1 
ATOM   3951 C CA  . MET   B 1 157 ? -30.734 6.650   -7.139  1.00 44.43  ? 154 MET   B CA  1 
ATOM   3952 C C   . MET   B 1 157 ? -30.683 5.130   -7.135  1.00 44.68  ? 154 MET   B C   1 
ATOM   3953 O O   . MET   B 1 157 ? -30.765 4.482   -8.187  1.00 35.40  ? 154 MET   B O   1 
ATOM   3954 C CB  . MET   B 1 157 ? -32.186 7.134   -7.112  1.00 41.96  ? 154 MET   B CB  1 
ATOM   3955 C CG  . MET   B 1 157 ? -32.367 8.519   -6.521  1.00 37.62  ? 154 MET   B CG  1 
ATOM   3956 S SD  . MET   B 1 157 ? -34.110 8.963   -6.451  1.00 53.78  ? 154 MET   B SD  1 
ATOM   3957 C CE  . MET   B 1 157 ? -34.022 10.605  -5.755  1.00 41.80  ? 154 MET   B CE  1 
ATOM   3958 N N   . GLN   B 1 158 ? -30.514 4.567   -5.939  1.00 45.66  ? 155 GLN   B N   1 
ATOM   3959 C CA  . GLN   B 1 158 ? -30.503 3.121   -5.714  1.00 45.76  ? 155 GLN   B CA  1 
ATOM   3960 C C   . GLN   B 1 158 ? -31.669 2.786   -4.790  1.00 44.81  ? 155 GLN   B C   1 
ATOM   3961 O O   . GLN   B 1 158 ? -31.505 2.624   -3.582  1.00 52.12  ? 155 GLN   B O   1 
ATOM   3962 C CB  . GLN   B 1 158 ? -29.191 2.692   -5.135  1.00 46.83  ? 155 GLN   B CB  1 
ATOM   3963 C CG  . GLN   B 1 158 ? -27.998 3.050   -5.991  1.00 51.62  ? 155 GLN   B CG  1 
ATOM   3964 C CD  . GLN   B 1 158 ? -26.708 2.435   -5.463  1.00 64.54  ? 155 GLN   B CD  1 
ATOM   3965 O OE1 . GLN   B 1 158 ? -26.680 1.849   -4.375  1.00 67.09  ? 155 GLN   B OE1 1 
ATOM   3966 N NE2 . GLN   B 1 158 ? -25.631 2.561   -6.238  1.00 63.94  ? 155 GLN   B NE2 1 
ATOM   3967 N N   . VAL   B 1 159 ? -32.860 2.701   -5.363  1.00 51.53  ? 156 VAL   B N   1 
ATOM   3968 C CA  . VAL   B 1 159 ? -34.067 2.463   -4.580  1.00 48.01  ? 156 VAL   B CA  1 
ATOM   3969 C C   . VAL   B 1 159 ? -34.083 1.004   -4.149  1.00 50.52  ? 156 VAL   B C   1 
ATOM   3970 O O   . VAL   B 1 159 ? -33.839 0.096   -4.958  1.00 46.90  ? 156 VAL   B O   1 
ATOM   3971 C CB  . VAL   B 1 159 ? -35.319 2.838   -5.389  1.00 46.35  ? 156 VAL   B CB  1 
ATOM   3972 C CG1 . VAL   B 1 159 ? -36.563 2.794   -4.512  1.00 50.95  ? 156 VAL   B CG1 1 
ATOM   3973 C CG2 . VAL   B 1 159 ? -35.146 4.221   -6.003  1.00 43.52  ? 156 VAL   B CG2 1 
ATOM   3974 N N   . ARG   B 1 160 ? -34.349 0.776   -2.880  1.00 47.78  ? 157 ARG   B N   1 
ATOM   3975 C CA  . ARG   B 1 160 ? -34.332 -0.574  -2.354  1.00 53.41  ? 157 ARG   B CA  1 
ATOM   3976 C C   . ARG   B 1 160 ? -35.617 -0.921  -1.622  1.00 50.24  ? 157 ARG   B C   1 
ATOM   3977 O O   . ARG   B 1 160 ? -36.276 -0.055  -1.074  1.00 46.48  ? 157 ARG   B O   1 
ATOM   3978 C CB  . ARG   B 1 160 ? -33.143 -0.731  -1.424  1.00 51.63  ? 157 ARG   B CB  1 
ATOM   3979 C CG  . ARG   B 1 160 ? -31.808 -0.725  -2.132  1.00 51.09  ? 157 ARG   B CG  1 
ATOM   3980 C CD  . ARG   B 1 160 ? -30.692 -0.504  -1.134  1.00 61.02  ? 157 ARG   B CD  1 
ATOM   3981 N NE  . ARG   B 1 160 ? -30.399 0.911   -0.966  1.00 64.76  ? 157 ARG   B NE  1 
ATOM   3982 C CZ  . ARG   B 1 160 ? -29.285 1.492   -1.389  1.00 64.98  ? 157 ARG   B CZ  1 
ATOM   3983 N NH1 . ARG   B 1 160 ? -28.353 0.781   -2.004  1.00 61.64  ? 157 ARG   B NH1 1 
ATOM   3984 N NH2 . ARG   B 1 160 ? -29.105 2.784   -1.194  1.00 61.25  ? 157 ARG   B NH2 1 
ATOM   3985 N N   . PRO   B 1 161 ? -35.986 -2.207  -1.644  1.00 52.11  ? 158 PRO   B N   1 
ATOM   3986 C CA  . PRO   B 1 161 ? -37.244 -2.617  -0.998  1.00 44.78  ? 158 PRO   B CA  1 
ATOM   3987 C C   . PRO   B 1 161 ? -37.356 -2.051  0.401   1.00 41.56  ? 158 PRO   B C   1 
ATOM   3988 O O   . PRO   B 1 161 ? -36.457 -2.242  1.222   1.00 47.81  ? 158 PRO   B O   1 
ATOM   3989 C CB  . PRO   B 1 161 ? -37.148 -4.145  -0.990  1.00 42.02  ? 158 PRO   B CB  1 
ATOM   3990 C CG  . PRO   B 1 161 ? -36.307 -4.475  -2.203  1.00 42.97  ? 158 PRO   B CG  1 
ATOM   3991 C CD  . PRO   B 1 161 ? -35.340 -3.322  -2.375  1.00 49.74  ? 158 PRO   B CD  1 
ATOM   3992 N N   . GLY   B 1 162 ? -38.414 -1.302  0.668   1.00 41.36  ? 159 GLY   B N   1 
ATOM   3993 C CA  . GLY   B 1 162 ? -38.617 -0.704  1.971   1.00 40.45  ? 159 GLY   B CA  1 
ATOM   3994 C C   . GLY   B 1 162 ? -38.325 0.779   2.070   1.00 45.32  ? 159 GLY   B C   1 
ATOM   3995 O O   . GLY   B 1 162 ? -38.646 1.376   3.106   1.00 45.98  ? 159 GLY   B O   1 
ATOM   3996 N N   . ASP   B 1 163 ? -37.729 1.395   1.040   1.00 46.71  ? 160 ASP   B N   1 
ATOM   3997 C CA  . ASP   B 1 163 ? -37.500 2.841   1.049   1.00 47.62  ? 160 ASP   B CA  1 
ATOM   3998 C C   . ASP   B 1 163 ? -38.822 3.601   1.098   1.00 45.03  ? 160 ASP   B C   1 
ATOM   3999 O O   . ASP   B 1 163 ? -39.878 3.086   0.713   1.00 46.30  ? 160 ASP   B O   1 
ATOM   4000 C CB  . ASP   B 1 163 ? -36.735 3.285   -0.203  1.00 46.73  ? 160 ASP   B CB  1 
ATOM   4001 C CG  . ASP   B 1 163 ? -35.265 2.940   -0.153  1.00 47.57  ? 160 ASP   B CG  1 
ATOM   4002 O OD1 . ASP   B 1 163 ? -34.661 3.065   0.933   1.00 49.59  ? 160 ASP   B OD1 1 
ATOM   4003 O OD2 . ASP   B 1 163 ? -34.719 2.547   -1.206  1.00 47.92  ? 160 ASP   B OD2 1 
ATOM   4004 N N   . THR   B 1 164 ? -38.767 4.855   1.555   1.00 43.02  ? 161 THR   B N   1 
ATOM   4005 C CA  . THR   B 1 164 ? -39.883 5.776   1.329   1.00 45.79  ? 161 THR   B CA  1 
ATOM   4006 C C   . THR   B 1 164 ? -39.368 6.898   0.412   1.00 51.53  ? 161 THR   B C   1 
ATOM   4007 O O   . THR   B 1 164 ? -38.619 7.788   0.838   1.00 48.33  ? 161 THR   B O   1 
ATOM   4008 C CB  . THR   B 1 164 ? -40.506 6.273   2.642   1.00 49.07  ? 161 THR   B CB  1 
ATOM   4009 O OG1 . THR   B 1 164 ? -39.783 7.393   3.165   1.00 60.83  ? 161 THR   B OG1 1 
ATOM   4010 C CG2 . THR   B 1 164 ? -40.535 5.142   3.679   1.00 50.11  ? 161 THR   B CG2 1 
ATOM   4011 N N   . VAL   B 1 165 ? -39.754 6.809   -0.871  1.00 45.87  ? 162 VAL   B N   1 
ATOM   4012 C CA  . VAL   B 1 165 ? -39.384 7.769   -1.907  1.00 46.33  ? 162 VAL   B CA  1 
ATOM   4013 C C   . VAL   B 1 165 ? -40.413 8.890   -1.942  1.00 45.21  ? 162 VAL   B C   1 
ATOM   4014 O O   . VAL   B 1 165 ? -41.605 8.625   -2.107  1.00 49.40  ? 162 VAL   B O   1 
ATOM   4015 C CB  . VAL   B 1 165 ? -39.301 7.077   -3.281  1.00 52.61  ? 162 VAL   B CB  1 
ATOM   4016 C CG1 . VAL   B 1 165 ? -39.067 8.105   -4.392  1.00 47.95  ? 162 VAL   B CG1 1 
ATOM   4017 C CG2 . VAL   B 1 165 ? -38.232 5.964   -3.297  1.00 37.12  ? 162 VAL   B CG2 1 
ATOM   4018 N N   . VAL   B 1 166 ? -39.962 10.139  -1.799  1.00 46.72  ? 163 VAL   B N   1 
ATOM   4019 C CA  . VAL   B 1 166 ? -40.815 11.325  -1.916  1.00 43.17  ? 163 VAL   B CA  1 
ATOM   4020 C C   . VAL   B 1 166 ? -40.555 11.979  -3.270  1.00 46.82  ? 163 VAL   B C   1 
ATOM   4021 O O   . VAL   B 1 166 ? -39.401 12.078  -3.704  1.00 45.12  ? 163 VAL   B O   1 
ATOM   4022 C CB  . VAL   B 1 166 ? -40.566 12.322  -0.764  1.00 39.88  ? 163 VAL   B CB  1 
ATOM   4023 C CG1 . VAL   B 1 166 ? -41.292 13.645  -1.001  1.00 35.59  ? 163 VAL   B CG1 1 
ATOM   4024 C CG2 . VAL   B 1 166 ? -41.009 11.725  0.551   1.00 47.93  ? 163 VAL   B CG2 1 
ATOM   4025 N N   . VAL   B 1 167 ? -41.623 12.419  -3.944  1.00 47.12  ? 164 VAL   B N   1 
ATOM   4026 C CA  . VAL   B 1 167 ? -41.518 13.059  -5.262  1.00 48.01  ? 164 VAL   B CA  1 
ATOM   4027 C C   . VAL   B 1 167 ? -42.307 14.365  -5.265  1.00 47.74  ? 164 VAL   B C   1 
ATOM   4028 O O   . VAL   B 1 167 ? -43.542 14.344  -5.283  1.00 47.22  ? 164 VAL   B O   1 
ATOM   4029 C CB  . VAL   B 1 167 ? -42.008 12.149  -6.393  1.00 43.02  ? 164 VAL   B CB  1 
ATOM   4030 C CG1 . VAL   B 1 167 ? -41.977 12.910  -7.712  1.00 47.94  ? 164 VAL   B CG1 1 
ATOM   4031 C CG2 . VAL   B 1 167 ? -41.141 10.895  -6.483  1.00 44.07  ? 164 VAL   B CG2 1 
ATOM   4032 N N   . SER   B 1 168 ? -41.603 15.497  -5.297  1.00 48.19  ? 165 SER   B N   1 
ATOM   4033 C CA  . SER   B 1 168 ? -42.269 16.784  -5.463  1.00 50.85  ? 165 SER   B CA  1 
ATOM   4034 C C   . SER   B 1 168 ? -42.518 17.066  -6.950  1.00 50.47  ? 165 SER   B C   1 
ATOM   4035 O O   . SER   B 1 168 ? -41.662 16.809  -7.804  1.00 43.13  ? 165 SER   B O   1 
ATOM   4036 C CB  . SER   B 1 168 ? -41.442 17.907  -4.835  1.00 45.62  ? 165 SER   B CB  1 
ATOM   4037 O OG  . SER   B 1 168 ? -40.196 18.057  -5.499  1.00 46.05  ? 165 SER   B OG  1 
ATOM   4038 N N   . GLY   B 1 169 ? -43.708 17.593  -7.257  1.00 55.21  ? 166 GLY   B N   1 
ATOM   4039 C CA  . GLY   B 1 169 ? -44.133 17.753  -8.634  1.00 44.80  ? 166 GLY   B CA  1 
ATOM   4040 C C   . GLY   B 1 169 ? -44.335 16.407  -9.297  1.00 48.52  ? 166 GLY   B C   1 
ATOM   4041 O O   . GLY   B 1 169 ? -43.592 16.045  -10.210 1.00 51.92  ? 166 GLY   B O   1 
ATOM   4042 N N   . ALA   B 1 170 ? -45.333 15.647  -8.852  1.00 51.04  ? 167 ALA   B N   1 
ATOM   4043 C CA  . ALA   B 1 170 ? -45.428 14.251  -9.251  1.00 48.19  ? 167 ALA   B CA  1 
ATOM   4044 C C   . ALA   B 1 170 ? -46.499 13.968  -10.296 1.00 50.61  ? 167 ALA   B C   1 
ATOM   4045 O O   . ALA   B 1 170 ? -46.495 12.867  -10.852 1.00 51.33  ? 167 ALA   B O   1 
ATOM   4046 C CB  . ALA   B 1 170 ? -45.684 13.366  -8.026  1.00 52.85  ? 167 ALA   B CB  1 
ATOM   4047 N N   . SER   B 1 171 ? -47.372 14.909  -10.589 1.00 54.64  ? 168 SER   B N   1 
ATOM   4048 C CA  . SER   B 1 171 ? -48.433 14.714  -11.572 1.00 50.21  ? 168 SER   B CA  1 
ATOM   4049 C C   . SER   B 1 171 ? -47.951 14.570  -13.014 1.00 50.86  ? 168 SER   B C   1 
ATOM   4050 O O   . SER   B 1 171 ? -48.596 13.897  -13.799 1.00 53.04  ? 168 SER   B O   1 
ATOM   4051 C CB  . SER   B 1 171 ? -49.393 15.887  -11.471 1.00 43.62  ? 168 SER   B CB  1 
ATOM   4052 O OG  . SER   B 1 171 ? -48.892 16.881  -10.606 1.00 52.75  ? 168 SER   B OG  1 
ATOM   4053 N N   . GLY   B 1 172 ? -46.816 15.171  -13.359 1.00 50.77  ? 169 GLY   B N   1 
ATOM   4054 C CA  . GLY   B 1 172 ? -46.324 15.167  -14.727 1.00 43.95  ? 169 GLY   B CA  1 
ATOM   4055 C C   . GLY   B 1 172 ? -45.661 13.857  -15.106 1.00 47.12  ? 169 GLY   B C   1 
ATOM   4056 O O   . GLY   B 1 172 ? -45.504 12.945  -14.297 1.00 49.18  ? 169 GLY   B O   1 
ATOM   4057 N N   . MET   B 1 173 ? -45.242 13.769  -16.375 1.00 47.09  ? 170 MET   B N   1 
ATOM   4058 C CA  . MET   B 1 173 ? -44.689 12.506  -16.864 1.00 45.46  ? 170 MET   B CA  1 
ATOM   4059 C C   . MET   B 1 173 ? -43.411 12.117  -16.131 1.00 49.20  ? 170 MET   B C   1 
ATOM   4060 O O   . MET   B 1 173 ? -43.169 10.928  -15.903 1.00 46.37  ? 170 MET   B O   1 
ATOM   4061 C CB  . MET   B 1 173 ? -44.432 12.554  -18.370 1.00 49.99  ? 170 MET   B CB  1 
ATOM   4062 C CG  . MET   B 1 173 ? -43.569 11.383  -18.857 1.00 44.98  ? 170 MET   B CG  1 
ATOM   4063 S SD  . MET   B 1 173 ? -43.479 11.053  -20.622 1.00 58.26  ? 170 MET   B SD  1 
ATOM   4064 C CE  . MET   B 1 173 ? -45.114 10.377  -20.944 1.00 53.40  ? 170 MET   B CE  1 
ATOM   4065 N N   . ILE   B 1 174 ? -42.591 13.090  -15.736 1.00 48.27  ? 171 ILE   B N   1 
ATOM   4066 C CA  . ILE   B 1 174 ? -41.348 12.753  -15.048 1.00 46.44  ? 171 ILE   B CA  1 
ATOM   4067 C C   . ILE   B 1 174 ? -41.629 12.277  -13.619 1.00 49.02  ? 171 ILE   B C   1 
ATOM   4068 O O   . ILE   B 1 174 ? -41.107 11.245  -13.188 1.00 46.17  ? 171 ILE   B O   1 
ATOM   4069 C CB  . ILE   B 1 174 ? -40.365 13.937  -15.095 1.00 47.09  ? 171 ILE   B CB  1 
ATOM   4070 C CG1 . ILE   B 1 174 ? -39.735 14.004  -16.488 1.00 47.58  ? 171 ILE   B CG1 1 
ATOM   4071 C CG2 . ILE   B 1 174 ? -39.262 13.794  -14.034 1.00 43.90  ? 171 ILE   B CG2 1 
ATOM   4072 C CD1 . ILE   B 1 174 ? -39.171 15.351  -16.846 1.00 39.76  ? 171 ILE   B CD1 1 
ATOM   4073 N N   . GLY   B 1 175 ? -42.473 12.998  -12.874 1.00 44.04  ? 172 GLY   B N   1 
ATOM   4074 C CA  . GLY   B 1 175 ? -42.774 12.582  -11.507 1.00 47.23  ? 172 GLY   B CA  1 
ATOM   4075 C C   . GLY   B 1 175 ? -43.464 11.226  -11.421 1.00 50.97  ? 172 GLY   B C   1 
ATOM   4076 O O   . GLY   B 1 175 ? -43.060 10.357  -10.636 1.00 45.33  ? 172 GLY   B O   1 
ATOM   4077 N N   . THR   B 1 176 ? -44.517 11.024  -12.229 1.00 47.77  ? 173 THR   B N   1 
ATOM   4078 C CA  . THR   B 1 176 ? -45.203 9.736   -12.233 1.00 46.89  ? 173 THR   B CA  1 
ATOM   4079 C C   . THR   B 1 176 ? -44.286 8.617   -12.699 1.00 46.40  ? 173 THR   B C   1 
ATOM   4080 O O   . THR   B 1 176 ? -44.423 7.483   -12.236 1.00 54.19  ? 173 THR   B O   1 
ATOM   4081 C CB  . THR   B 1 176 ? -46.469 9.744   -13.121 1.00 49.52  ? 173 THR   B CB  1 
ATOM   4082 O OG1 . THR   B 1 176 ? -46.112 9.779   -14.507 1.00 45.59  ? 173 THR   B OG1 1 
ATOM   4083 C CG2 . THR   B 1 176 ? -47.385 10.902  -12.825 1.00 46.87  ? 173 THR   B CG2 1 
ATOM   4084 N N   . LEU   B 1 177 ? -43.375 8.893   -13.633 1.00 44.39  ? 174 LEU   B N   1 
ATOM   4085 C CA  . LEU   B 1 177 ? -42.439 7.853   -14.058 1.00 47.22  ? 174 LEU   B CA  1 
ATOM   4086 C C   . LEU   B 1 177 ? -41.510 7.447   -12.917 1.00 49.45  ? 174 LEU   B C   1 
ATOM   4087 O O   . LEU   B 1 177 ? -41.213 6.258   -12.740 1.00 49.17  ? 174 LEU   B O   1 
ATOM   4088 C CB  . LEU   B 1 177 ? -41.621 8.329   -15.256 1.00 47.25  ? 174 LEU   B CB  1 
ATOM   4089 C CG  . LEU   B 1 177 ? -42.031 7.854   -16.644 1.00 47.31  ? 174 LEU   B CG  1 
ATOM   4090 C CD1 . LEU   B 1 177 ? -41.218 8.563   -17.731 1.00 51.89  ? 174 LEU   B CD1 1 
ATOM   4091 C CD2 . LEU   B 1 177 ? -41.863 6.353   -16.774 1.00 55.94  ? 174 LEU   B CD2 1 
ATOM   4092 N N   . VAL   B 1 178 ? -41.050 8.425   -12.131 1.00 48.93  ? 175 VAL   B N   1 
ATOM   4093 C CA  . VAL   B 1 178 ? -40.185 8.136   -10.992 1.00 47.70  ? 175 VAL   B CA  1 
ATOM   4094 C C   . VAL   B 1 178 ? -40.921 7.273   -9.981  1.00 46.72  ? 175 VAL   B C   1 
ATOM   4095 O O   . VAL   B 1 178 ? -40.403 6.245   -9.536  1.00 47.98  ? 175 VAL   B O   1 
ATOM   4096 C CB  . VAL   B 1 178 ? -39.666 9.445   -10.362 1.00 45.05  ? 175 VAL   B CB  1 
ATOM   4097 C CG1 . VAL   B 1 178 ? -38.984 9.195   -9.007  1.00 43.27  ? 175 VAL   B CG1 1 
ATOM   4098 C CG2 . VAL   B 1 178 ? -38.694 10.116  -11.301 1.00 40.10  ? 175 VAL   B CG2 1 
ATOM   4099 N N   . GLY   B 1 179 ? -42.145 7.671   -9.618  1.00 46.96  ? 176 GLY   B N   1 
ATOM   4100 C CA  . GLY   B 1 179 ? -42.903 6.911   -8.630  1.00 48.81  ? 176 GLY   B CA  1 
ATOM   4101 C C   . GLY   B 1 179 ? -43.101 5.453   -9.018  1.00 52.69  ? 176 GLY   B C   1 
ATOM   4102 O O   . GLY   B 1 179 ? -42.956 4.550   -8.192  1.00 53.67  ? 176 GLY   B O   1 
ATOM   4103 N N   . GLN   B 1 180 ? -43.413 5.198   -10.283 1.00 49.70  ? 177 GLN   B N   1 
ATOM   4104 C CA  . GLN   B 1 180 ? -43.721 3.831   -10.684 1.00 54.33  ? 177 GLN   B CA  1 
ATOM   4105 C C   . GLN   B 1 180 ? -42.485 2.942   -10.664 1.00 53.17  ? 177 GLN   B C   1 
ATOM   4106 O O   . GLN   B 1 180 ? -42.569 1.768   -10.284 1.00 56.34  ? 177 GLN   B O   1 
ATOM   4107 C CB  . GLN   B 1 180 ? -44.361 3.822   -12.069 1.00 47.36  ? 177 GLN   B CB  1 
ATOM   4108 C CG  . GLN   B 1 180 ? -45.788 4.327   -12.087 1.00 55.36  ? 177 GLN   B CG  1 
ATOM   4109 C CD  . GLN   B 1 180 ? -46.447 4.069   -13.421 1.00 65.83  ? 177 GLN   B CD  1 
ATOM   4110 O OE1 . GLN   B 1 180 ? -45.789 4.075   -14.464 1.00 66.01  ? 177 GLN   B OE1 1 
ATOM   4111 N NE2 . GLN   B 1 180 ? -47.746 3.809   -13.394 1.00 74.98  ? 177 GLN   B NE2 1 
ATOM   4112 N N   . MET   B 1 181 ? -41.342 3.464   -11.116 1.00 50.56  ? 178 MET   B N   1 
ATOM   4113 C CA  . MET   B 1 181 ? -40.103 2.701   -11.040 1.00 50.00  ? 178 MET   B CA  1 
ATOM   4114 C C   . MET   B 1 181 ? -39.689 2.456   -9.595  1.00 49.62  ? 178 MET   B C   1 
ATOM   4115 O O   . MET   B 1 181 ? -39.162 1.386   -9.272  1.00 49.64  ? 178 MET   B O   1 
ATOM   4116 C CB  . MET   B 1 181 ? -39.005 3.436   -11.803 1.00 48.14  ? 178 MET   B CB  1 
ATOM   4117 C CG  . MET   B 1 181 ? -39.255 3.478   -13.285 1.00 46.02  ? 178 MET   B CG  1 
ATOM   4118 S SD  . MET   B 1 181 ? -38.000 4.384   -14.184 1.00 57.99  ? 178 MET   B SD  1 
ATOM   4119 C CE  . MET   B 1 181 ? -38.336 6.023   -13.538 1.00 49.71  ? 178 MET   B CE  1 
ATOM   4120 N N   . ALA   B 1 182 ? -39.937 3.432   -8.720  1.00 45.59  ? 179 ALA   B N   1 
ATOM   4121 C CA  . ALA   B 1 182 ? -39.643 3.286   -7.303  1.00 43.48  ? 179 ALA   B CA  1 
ATOM   4122 C C   . ALA   B 1 182 ? -40.529 2.223   -6.664  1.00 55.79  ? 179 ALA   B C   1 
ATOM   4123 O O   . ALA   B 1 182 ? -40.049 1.399   -5.871  1.00 52.10  ? 179 ALA   B O   1 
ATOM   4124 C CB  . ALA   B 1 182 ? -39.821 4.633   -6.607  1.00 44.12  ? 179 ALA   B CB  1 
ATOM   4125 N N   . LYS   B 1 183 ? -41.800 2.193   -7.024  1.00 56.97  ? 180 LYS   B N   1 
ATOM   4126 C CA  . LYS   B 1 183 ? -42.691 1.169   -6.523  1.00 51.93  ? 180 LYS   B CA  1 
ATOM   4127 C C   . LYS   B 1 183 ? -42.256 -0.192  -7.008  1.00 50.90  ? 180 LYS   B C   1 
ATOM   4128 O O   . LYS   B 1 183 ? -42.289 -1.150  -6.262  1.00 49.16  ? 180 LYS   B O   1 
ATOM   4129 C CB  . LYS   B 1 183 ? -44.098 1.458   -6.975  1.00 49.01  ? 180 LYS   B CB  1 
ATOM   4130 C CG  . LYS   B 1 183 ? -45.004 1.966   -5.878  1.00 58.49  ? 180 LYS   B CG  1 
ATOM   4131 C CD  . LYS   B 1 183 ? -45.420 0.824   -4.976  1.00 58.05  ? 180 LYS   B CD  1 
ATOM   4132 C CE  . LYS   B 1 183 ? -46.183 1.343   -3.779  1.00 54.04  ? 180 LYS   B CE  1 
ATOM   4133 N NZ  . LYS   B 1 183 ? -45.620 0.826   -2.505  1.00 68.88  ? 180 LYS   B NZ  1 
ATOM   4134 N N   . ARG   B 1 184 ? -41.832 -0.276  -8.257  1.00 49.89  ? 181 ARG   B N   1 
ATOM   4135 C CA  . ARG   B 1 184 ? -41.351 -1.547  -8.786  1.00 57.19  ? 181 ARG   B CA  1 
ATOM   4136 C C   . ARG   B 1 184 ? -40.104 -2.047  -8.062  1.00 53.27  ? 181 ARG   B C   1 
ATOM   4137 O O   . ARG   B 1 184 ? -39.840 -3.253  -8.074  1.00 55.18  ? 181 ARG   B O   1 
ATOM   4138 C CB  . ARG   B 1 184 ? -41.083 -1.423  -10.291 1.00 54.68  ? 181 ARG   B CB  1 
ATOM   4139 C CG  . ARG   B 1 184 ? -42.343 -1.214  -11.109 1.00 57.43  ? 181 ARG   B CG  1 
ATOM   4140 C CD  . ARG   B 1 184 ? -42.014 -1.131  -12.579 1.00 62.52  ? 181 ARG   B CD  1 
ATOM   4141 N NE  . ARG   B 1 184 ? -41.016 -2.120  -12.961 1.00 62.28  ? 181 ARG   B NE  1 
ATOM   4142 C CZ  . ARG   B 1 184 ? -41.296 -3.306  -13.482 1.00 62.53  ? 181 ARG   B CZ  1 
ATOM   4143 N NH1 . ARG   B 1 184 ? -42.548 -3.698  -13.676 1.00 59.89  ? 181 ARG   B NH1 1 
ATOM   4144 N NH2 . ARG   B 1 184 ? -40.296 -4.116  -13.823 1.00 57.52  ? 181 ARG   B NH2 1 
ATOM   4145 N N   . ALA   B 1 185 ? -39.340 -1.157  -7.431  1.00 49.14  ? 182 ALA   B N   1 
ATOM   4146 C CA  . ALA   B 1 185 ? -38.176 -1.548  -6.647  1.00 51.93  ? 182 ALA   B CA  1 
ATOM   4147 C C   . ALA   B 1 185 ? -38.508 -1.789  -5.171  1.00 56.83  ? 182 ALA   B C   1 
ATOM   4148 O O   . ALA   B 1 185 ? -37.596 -2.066  -4.378  1.00 51.94  ? 182 ALA   B O   1 
ATOM   4149 C CB  . ALA   B 1 185 ? -37.075 -0.486  -6.774  1.00 45.21  ? 182 ALA   B CB  1 
ATOM   4150 N N   . GLY   B 1 186 ? -39.778 -1.687  -4.787  1.00 50.03  ? 183 GLY   B N   1 
ATOM   4151 C CA  . GLY   B 1 186 ? -40.201 -1.993  -3.446  1.00 38.83  ? 183 GLY   B CA  1 
ATOM   4152 C C   . GLY   B 1 186 ? -40.452 -0.808  -2.552  1.00 45.96  ? 183 GLY   B C   1 
ATOM   4153 O O   . GLY   B 1 186 ? -40.662 -0.997  -1.351  1.00 55.69  ? 183 GLY   B O   1 
ATOM   4154 N N   . ALA   B 1 187 ? -40.468 0.397   -3.077  1.00 44.81  ? 184 ALA   B N   1 
ATOM   4155 C CA  . ALA   B 1 187 ? -40.539 1.545   -2.190  1.00 48.82  ? 184 ALA   B CA  1 
ATOM   4156 C C   . ALA   B 1 187 ? -41.976 1.943   -1.875  1.00 45.27  ? 184 ALA   B C   1 
ATOM   4157 O O   . ALA   B 1 187 ? -42.905 1.672   -2.641  1.00 47.17  ? 184 ALA   B O   1 
ATOM   4158 C CB  . ALA   B 1 187 ? -39.800 2.738   -2.799  1.00 51.39  ? 184 ALA   B CB  1 
ATOM   4159 N N   . ARG   B 1 188 ? -42.146 2.576   -0.718  1.00 39.69  ? 185 ARG   B N   1 
ATOM   4160 C CA  . ARG   B 1 188 ? -43.270 3.472   -0.495  1.00 44.77  ? 185 ARG   B CA  1 
ATOM   4161 C C   . ARG   B 1 188 ? -43.003 4.772   -1.250  1.00 52.67  ? 185 ARG   B C   1 
ATOM   4162 O O   . ARG   B 1 188 ? -41.897 5.319   -1.179  1.00 47.51  ? 185 ARG   B O   1 
ATOM   4163 C CB  . ARG   B 1 188 ? -43.443 3.747   0.996   1.00 44.85  ? 185 ARG   B CB  1 
ATOM   4164 C CG  . ARG   B 1 188 ? -44.419 4.857   1.350   1.00 45.65  ? 185 ARG   B CG  1 
ATOM   4165 C CD  . ARG   B 1 188 ? -44.471 5.014   2.869   1.00 44.34  ? 185 ARG   B CD  1 
ATOM   4166 N NE  . ARG   B 1 188 ? -45.463 5.979   3.332   1.00 48.85  ? 185 ARG   B NE  1 
ATOM   4167 C CZ  . ARG   B 1 188 ? -46.756 5.717   3.490   1.00 55.64  ? 185 ARG   B CZ  1 
ATOM   4168 N NH1 . ARG   B 1 188 ? -47.267 4.530   3.180   1.00 47.28  ? 185 ARG   B NH1 1 
ATOM   4169 N NH2 . ARG   B 1 188 ? -47.557 6.671   3.966   1.00 50.56  ? 185 ARG   B NH2 1 
ATOM   4170 N N   . VAL   B 1 189 ? -44.002 5.263   -1.983  1.00 52.29  ? 186 VAL   B N   1 
ATOM   4171 C CA  . VAL   B 1 189 ? -43.837 6.426   -2.849  1.00 47.97  ? 186 VAL   B CA  1 
ATOM   4172 C C   . VAL   B 1 189 ? -44.853 7.495   -2.461  1.00 49.96  ? 186 VAL   B C   1 
ATOM   4173 O O   . VAL   B 1 189 ? -46.059 7.236   -2.431  1.00 52.45  ? 186 VAL   B O   1 
ATOM   4174 C CB  . VAL   B 1 189 ? -43.969 6.052   -4.327  1.00 49.53  ? 186 VAL   B CB  1 
ATOM   4175 C CG1 . VAL   B 1 189 ? -43.911 7.305   -5.178  1.00 50.33  ? 186 VAL   B CG1 1 
ATOM   4176 C CG2 . VAL   B 1 189 ? -42.884 5.054   -4.717  1.00 47.39  ? 186 VAL   B CG2 1 
ATOM   4177 N N   . VAL   B 1 190 ? -44.363 8.693   -2.165  1.00 51.66  ? 187 VAL   B N   1 
ATOM   4178 C CA  . VAL   B 1 190 ? -45.194 9.836   -1.813  1.00 47.24  ? 187 VAL   B CA  1 
ATOM   4179 C C   . VAL   B 1 190 ? -44.985 10.917  -2.863  1.00 52.70  ? 187 VAL   B C   1 
ATOM   4180 O O   . VAL   B 1 190 ? -43.842 11.260  -3.185  1.00 49.50  ? 187 VAL   B O   1 
ATOM   4181 C CB  . VAL   B 1 190 ? -44.850 10.375  -0.418  1.00 40.40  ? 187 VAL   B CB  1 
ATOM   4182 C CG1 . VAL   B 1 190 ? -45.823 11.459  -0.034  1.00 46.06  ? 187 VAL   B CG1 1 
ATOM   4183 C CG2 . VAL   B 1 190 ? -44.864 9.252   0.586   1.00 52.19  ? 187 VAL   B CG2 1 
ATOM   4184 N N   . GLY   B 1 191 ? -46.084 11.450  -3.398  1.00 57.34  ? 188 GLY   B N   1 
ATOM   4185 C CA  . GLY   B 1 191 ? -46.039 12.575  -4.302  1.00 50.11  ? 188 GLY   B CA  1 
ATOM   4186 C C   . GLY   B 1 191 ? -46.663 13.841  -3.726  1.00 53.40  ? 188 GLY   B C   1 
ATOM   4187 O O   . GLY   B 1 191 ? -47.181 13.887  -2.609  1.00 49.90  ? 188 GLY   B O   1 
ATOM   4188 N N   . THR   B 1 192 ? -46.574 14.901  -4.528  1.00 57.37  ? 189 THR   B N   1 
ATOM   4189 C CA  . THR   B 1 192 ? -47.449 16.058  -4.403  1.00 60.20  ? 189 THR   B CA  1 
ATOM   4190 C C   . THR   B 1 192 ? -48.219 16.218  -5.708  1.00 57.55  ? 189 THR   B C   1 
ATOM   4191 O O   . THR   B 1 192 ? -47.823 15.690  -6.752  1.00 54.37  ? 189 THR   B O   1 
ATOM   4192 C CB  . THR   B 1 192 ? -46.680 17.351  -4.079  1.00 58.57  ? 189 THR   B CB  1 
ATOM   4193 O OG1 . THR   B 1 192 ? -45.791 17.674  -5.158  1.00 59.67  ? 189 THR   B OG1 1 
ATOM   4194 C CG2 . THR   B 1 192 ? -45.893 17.194  -2.785  1.00 55.71  ? 189 THR   B CG2 1 
ATOM   4195 N N   . ALA   B 1 193 ? -49.343 16.930  -5.625  1.00 58.77  ? 190 ALA   B N   1 
ATOM   4196 C CA  . ALA   B 1 193 ? -50.154 17.260  -6.791  1.00 53.12  ? 190 ALA   B CA  1 
ATOM   4197 C C   . ALA   B 1 193 ? -51.131 18.359  -6.392  1.00 56.25  ? 190 ALA   B C   1 
ATOM   4198 O O   . ALA   B 1 193 ? -51.303 18.668  -5.208  1.00 57.70  ? 190 ALA   B O   1 
ATOM   4199 C CB  . ALA   B 1 193 ? -50.883 16.029  -7.348  1.00 58.22  ? 190 ALA   B CB  1 
ATOM   4200 N N   . GLY   B 1 194 ? -51.770 18.953  -7.402  1.00 59.37  ? 191 GLY   B N   1 
ATOM   4201 C CA  . GLY   B 1 194 ? -52.526 20.179  -7.210  1.00 56.72  ? 191 GLY   B CA  1 
ATOM   4202 C C   . GLY   B 1 194 ? -54.024 20.022  -7.083  1.00 61.50  ? 191 GLY   B C   1 
ATOM   4203 O O   . GLY   B 1 194 ? -54.694 20.829  -6.425  1.00 62.14  ? 191 GLY   B O   1 
ATOM   4204 N N   . SER   B 1 195 ? -54.566 18.987  -7.707  1.00 57.95  ? 192 SER   B N   1 
ATOM   4205 C CA  . SER   B 1 195 ? -56.000 18.766  -7.708  1.00 65.02  ? 192 SER   B CA  1 
ATOM   4206 C C   . SER   B 1 195 ? -56.336 17.542  -6.863  1.00 72.89  ? 192 SER   B C   1 
ATOM   4207 O O   . SER   B 1 195 ? -55.522 16.621  -6.719  1.00 72.56  ? 192 SER   B O   1 
ATOM   4208 C CB  . SER   B 1 195 ? -56.520 18.575  -9.133  1.00 62.57  ? 192 SER   B CB  1 
ATOM   4209 O OG  . SER   B 1 195 ? -56.360 17.228  -9.533  1.00 67.47  ? 192 SER   B OG  1 
ATOM   4210 N N   . ALA   B 1 196 ? -57.543 17.543  -6.294  1.00 69.06  ? 193 ALA   B N   1 
ATOM   4211 C CA  . ALA   B 1 196 ? -58.071 16.301  -5.748  1.00 63.18  ? 193 ALA   B CA  1 
ATOM   4212 C C   . ALA   B 1 196 ? -58.146 15.222  -6.822  1.00 65.47  ? 193 ALA   B C   1 
ATOM   4213 O O   . ALA   B 1 196 ? -57.932 14.036  -6.534  1.00 62.37  ? 193 ALA   B O   1 
ATOM   4214 C CB  . ALA   B 1 196 ? -59.446 16.543  -5.134  1.00 61.03  ? 193 ALA   B CB  1 
ATOM   4215 N N   . GLY   B 1 197 ? -58.406 15.618  -8.072  1.00 63.83  ? 194 GLY   B N   1 
ATOM   4216 C CA  . GLY   B 1 197 ? -58.569 14.646  -9.138  1.00 58.75  ? 194 GLY   B CA  1 
ATOM   4217 C C   . GLY   B 1 197 ? -57.264 14.047  -9.615  1.00 67.71  ? 194 GLY   B C   1 
ATOM   4218 O O   . GLY   B 1 197 ? -57.245 12.923  -10.129 1.00 70.30  ? 194 GLY   B O   1 
ATOM   4219 N N   . LYS   B 1 198 ? -56.160 14.786  -9.482  1.00 69.49  ? 195 LYS   B N   1 
ATOM   4220 C CA  . LYS   B 1 198 ? -54.861 14.221  -9.839  1.00 68.83  ? 195 LYS   B CA  1 
ATOM   4221 C C   . LYS   B 1 198 ? -54.292 13.388  -8.702  1.00 66.06  ? 195 LYS   B C   1 
ATOM   4222 O O   . LYS   B 1 198 ? -53.626 12.375  -8.956  1.00 59.04  ? 195 LYS   B O   1 
ATOM   4223 C CB  . LYS   B 1 198 ? -53.879 15.330  -10.230 1.00 64.99  ? 195 LYS   B CB  1 
ATOM   4224 C CG  . LYS   B 1 198 ? -53.983 15.759  -11.680 1.00 57.19  ? 195 LYS   B CG  1 
ATOM   4225 C CD  . LYS   B 1 198 ? -52.877 16.715  -12.019 1.00 58.03  ? 195 LYS   B CD  1 
ATOM   4226 C CE  . LYS   B 1 198 ? -52.874 17.075  -13.493 1.00 61.91  ? 195 LYS   B CE  1 
ATOM   4227 N NZ  . LYS   B 1 198 ? -51.635 17.825  -13.850 1.00 53.53  ? 195 LYS   B NZ  1 
ATOM   4228 N N   . ALA   B 1 199 ? -54.550 13.808  -7.457  1.00 64.98  ? 196 ALA   B N   1 
ATOM   4229 C CA  . ALA   B 1 199 ? -54.228 12.991  -6.290  1.00 63.68  ? 196 ALA   B CA  1 
ATOM   4230 C C   . ALA   B 1 199 ? -54.769 11.575  -6.440  1.00 66.86  ? 196 ALA   B C   1 
ATOM   4231 O O   . ALA   B 1 199 ? -54.062 10.591  -6.170  1.00 66.19  ? 196 ALA   B O   1 
ATOM   4232 C CB  . ALA   B 1 199 ? -54.791 13.653  -5.030  1.00 58.26  ? 196 ALA   B CB  1 
ATOM   4233 N N   . ARG   B 1 200 ? -56.026 11.455  -6.882  1.00 65.93  ? 197 ARG   B N   1 
ATOM   4234 C CA  . ARG   B 1 200 ? -56.639 10.158  -7.154  1.00 66.08  ? 197 ARG   B CA  1 
ATOM   4235 C C   . ARG   B 1 200 ? -56.078 9.504   -8.412  1.00 62.94  ? 197 ARG   B C   1 
ATOM   4236 O O   . ARG   B 1 200 ? -56.069 8.271   -8.512  1.00 62.75  ? 197 ARG   B O   1 
ATOM   4237 C CB  . ARG   B 1 200 ? -58.162 10.344  -7.233  1.00 66.57  ? 197 ARG   B CB  1 
ATOM   4238 C CG  . ARG   B 1 200 ? -58.946 9.395   -8.154  1.00 70.10  ? 197 ARG   B CG  1 
ATOM   4239 C CD  . ARG   B 1 200 ? -60.475 9.640   -8.076  1.00 70.43  ? 197 ARG   B CD  1 
ATOM   4240 N NE  . ARG   B 1 200 ? -60.866 11.008  -8.419  1.00 70.47  ? 197 ARG   B NE  1 
ATOM   4241 C CZ  . ARG   B 1 200 ? -61.084 11.982  -7.541  1.00 65.22  ? 197 ARG   B CZ  1 
ATOM   4242 N NH1 . ARG   B 1 200 ? -60.961 11.783  -6.237  1.00 58.37  ? 197 ARG   B NH1 1 
ATOM   4243 N NH2 . ARG   B 1 200 ? -61.430 13.191  -7.982  1.00 63.57  ? 197 ARG   B NH2 1 
ATOM   4244 N N   . TYR   B 1 201 ? -55.580 10.303  -9.359  1.00 65.84  ? 198 TYR   B N   1 
ATOM   4245 C CA  . TYR   B 1 201 ? -54.893 9.744   -10.517 1.00 60.30  ? 198 TYR   B CA  1 
ATOM   4246 C C   . TYR   B 1 201 ? -53.557 9.124   -10.110 1.00 63.13  ? 198 TYR   B C   1 
ATOM   4247 O O   . TYR   B 1 201 ? -53.232 8.002   -10.524 1.00 62.11  ? 198 TYR   B O   1 
ATOM   4248 C CB  . TYR   B 1 201 ? -54.715 10.839  -11.576 1.00 58.85  ? 198 TYR   B CB  1 
ATOM   4249 C CG  . TYR   B 1 201 ? -53.821 10.471  -12.746 1.00 56.71  ? 198 TYR   B CG  1 
ATOM   4250 C CD1 . TYR   B 1 201 ? -54.199 9.496   -13.654 1.00 59.07  ? 198 TYR   B CD1 1 
ATOM   4251 C CD2 . TYR   B 1 201 ? -52.605 11.116  -12.948 1.00 58.39  ? 198 TYR   B CD2 1 
ATOM   4252 C CE1 . TYR   B 1 201 ? -53.389 9.160   -14.727 1.00 61.01  ? 198 TYR   B CE1 1 
ATOM   4253 C CE2 . TYR   B 1 201 ? -51.787 10.788  -14.018 1.00 58.32  ? 198 TYR   B CE2 1 
ATOM   4254 C CZ  . TYR   B 1 201 ? -52.186 9.809   -14.904 1.00 62.41  ? 198 TYR   B CZ  1 
ATOM   4255 O OH  . TYR   B 1 201 ? -51.387 9.472   -15.975 1.00 61.97  ? 198 TYR   B OH  1 
ATOM   4256 N N   . LEU   B 1 202 ? -52.781 9.828   -9.277  1.00 60.58  ? 199 LEU   B N   1 
ATOM   4257 C CA  . LEU   B 1 202 ? -51.493 9.306   -8.823  1.00 59.01  ? 199 LEU   B CA  1 
ATOM   4258 C C   . LEU   B 1 202 ? -51.660 8.057   -7.969  1.00 61.25  ? 199 LEU   B C   1 
ATOM   4259 O O   . LEU   B 1 202 ? -50.928 7.075   -8.142  1.00 57.62  ? 199 LEU   B O   1 
ATOM   4260 C CB  . LEU   B 1 202 ? -50.745 10.378  -8.037  1.00 59.64  ? 199 LEU   B CB  1 
ATOM   4261 C CG  . LEU   B 1 202 ? -50.121 11.474  -8.892  1.00 51.92  ? 199 LEU   B CG  1 
ATOM   4262 C CD1 . LEU   B 1 202 ? -49.254 12.369  -8.041  1.00 49.53  ? 199 LEU   B CD1 1 
ATOM   4263 C CD2 . LEU   B 1 202 ? -49.333 10.830  -10.013 1.00 52.19  ? 199 LEU   B CD2 1 
ATOM   4264 N N   . SER   B 1 203 ? -52.600 8.089   -7.018  1.00 61.27  ? 200 SER   B N   1 
ATOM   4265 C CA  . SER   B 1 203 ? -52.883 6.902   -6.216  1.00 59.69  ? 200 SER   B CA  1 
ATOM   4266 C C   . SER   B 1 203 ? -53.142 5.691   -7.104  1.00 60.58  ? 200 SER   B C   1 
ATOM   4267 O O   . SER   B 1 203 ? -52.493 4.648   -6.958  1.00 59.16  ? 200 SER   B O   1 
ATOM   4268 C CB  . SER   B 1 203 ? -54.069 7.162   -5.287  1.00 57.42  ? 200 SER   B CB  1 
ATOM   4269 O OG  . SER   B 1 203 ? -53.787 8.244   -4.412  1.00 57.99  ? 200 SER   B OG  1 
ATOM   4270 N N   . GLN   B 1 204 ? -54.052 5.831   -8.074  1.00 57.56  ? 201 GLN   B N   1 
ATOM   4271 C CA  . GLN   B 1 204 ? -54.380 4.703   -8.939  1.00 59.18  ? 201 GLN   B CA  1 
ATOM   4272 C C   . GLN   B 1 204 ? -53.206 4.264   -9.798  1.00 63.19  ? 201 GLN   B C   1 
ATOM   4273 O O   . GLN   B 1 204 ? -53.310 3.238   -10.480 1.00 65.42  ? 201 GLN   B O   1 
ATOM   4274 C CB  . GLN   B 1 204 ? -55.580 5.041   -9.826  1.00 67.11  ? 201 GLN   B CB  1 
ATOM   4275 C CG  . GLN   B 1 204 ? -56.877 5.208   -9.041  1.00 70.82  ? 201 GLN   B CG  1 
ATOM   4276 C CD  . GLN   B 1 204 ? -58.123 4.887   -9.849  1.00 71.49  ? 201 GLN   B CD  1 
ATOM   4277 O OE1 . GLN   B 1 204 ? -58.094 4.087   -10.797 1.00 69.73  ? 201 GLN   B OE1 1 
ATOM   4278 N NE2 . GLN   B 1 204 ? -59.236 5.509   -9.470  1.00 70.37  ? 201 GLN   B NE2 1 
ATOM   4279 N N   . LEU   B 1 205 ? -52.109 5.017   -9.795  1.00 66.84  ? 202 LEU   B N   1 
ATOM   4280 C CA  . LEU   B 1 205 ? -50.876 4.621   -10.458 1.00 61.98  ? 202 LEU   B CA  1 
ATOM   4281 C C   . LEU   B 1 205 ? -49.915 3.921   -9.514  1.00 65.11  ? 202 LEU   B C   1 
ATOM   4282 O O   . LEU   B 1 205 ? -48.872 3.435   -9.963  1.00 70.03  ? 202 LEU   B O   1 
ATOM   4283 C CB  . LEU   B 1 205 ? -50.197 5.844   -11.081 1.00 63.19  ? 202 LEU   B CB  1 
ATOM   4284 C CG  . LEU   B 1 205 ? -50.886 6.402   -12.331 1.00 64.47  ? 202 LEU   B CG  1 
ATOM   4285 C CD1 . LEU   B 1 205 ? -50.540 7.858   -12.587 1.00 58.99  ? 202 LEU   B CD1 1 
ATOM   4286 C CD2 . LEU   B 1 205 ? -50.495 5.570   -13.511 1.00 60.05  ? 202 LEU   B CD2 1 
ATOM   4287 N N   . GLY   B 1 206 ? -50.248 3.850   -8.226  1.00 65.27  ? 203 GLY   B N   1 
ATOM   4288 C CA  . GLY   B 1 206 ? -49.428 3.186   -7.226  1.00 62.34  ? 203 GLY   B CA  1 
ATOM   4289 C C   . GLY   B 1 206 ? -48.936 4.078   -6.101  1.00 61.17  ? 203 GLY   B C   1 
ATOM   4290 O O   . GLY   B 1 206 ? -48.266 3.572   -5.191  1.00 58.66  ? 203 GLY   B O   1 
ATOM   4291 N N   . PHE   B 1 207 ? -49.221 5.382   -6.106  1.00 60.78  ? 204 PHE   B N   1 
ATOM   4292 C CA  . PHE   B 1 207 ? -48.724 6.263   -5.055  1.00 56.73  ? 204 PHE   B CA  1 
ATOM   4293 C C   . PHE   B 1 207 ? -49.424 5.958   -3.735  1.00 58.22  ? 204 PHE   B C   1 
ATOM   4294 O O   . PHE   B 1 207 ? -50.656 5.901   -3.672  1.00 62.71  ? 204 PHE   B O   1 
ATOM   4295 C CB  . PHE   B 1 207 ? -48.941 7.724   -5.443  1.00 57.75  ? 204 PHE   B CB  1 
ATOM   4296 C CG  . PHE   B 1 207 ? -47.844 8.303   -6.307  1.00 59.63  ? 204 PHE   B CG  1 
ATOM   4297 C CD1 . PHE   B 1 207 ? -47.517 7.726   -7.527  1.00 53.53  ? 204 PHE   B CD1 1 
ATOM   4298 C CD2 . PHE   B 1 207 ? -47.150 9.441   -5.902  1.00 58.02  ? 204 PHE   B CD2 1 
ATOM   4299 C CE1 . PHE   B 1 207 ? -46.517 8.258   -8.315  1.00 47.93  ? 204 PHE   B CE1 1 
ATOM   4300 C CE2 . PHE   B 1 207 ? -46.153 9.982   -6.694  1.00 53.59  ? 204 PHE   B CE2 1 
ATOM   4301 C CZ  . PHE   B 1 207 ? -45.839 9.389   -7.902  1.00 51.71  ? 204 PHE   B CZ  1 
ATOM   4302 N N   . ASP   B 1 208 ? -48.635 5.769   -2.676  1.00 55.47  ? 205 ASP   B N   1 
ATOM   4303 C CA  . ASP   B 1 208 ? -49.192 5.424   -1.371  1.00 55.80  ? 205 ASP   B CA  1 
ATOM   4304 C C   . ASP   B 1 208 ? -49.714 6.637   -0.615  1.00 54.71  ? 205 ASP   B C   1 
ATOM   4305 O O   . ASP   B 1 208 ? -50.452 6.462   0.358   1.00 56.51  ? 205 ASP   B O   1 
ATOM   4306 C CB  . ASP   B 1 208 ? -48.144 4.685   -0.530  1.00 48.30  ? 205 ASP   B CB  1 
ATOM   4307 C CG  . ASP   B 1 208 ? -47.541 3.483   -1.272  1.00 56.02  ? 205 ASP   B CG  1 
ATOM   4308 O OD1 . ASP   B 1 208 ? -48.292 2.574   -1.699  1.00 58.60  ? 205 ASP   B OD1 1 
ATOM   4309 O OD2 . ASP   B 1 208 ? -46.309 3.464   -1.466  1.00 55.76  ? 205 ASP   B OD2 1 
ATOM   4310 N N   . ALA   B 1 209 ? -49.368 7.851   -1.046  1.00 54.01  ? 206 ALA   B N   1 
ATOM   4311 C CA  . ALA   B 1 209 ? -49.894 9.077   -0.459  1.00 50.80  ? 206 ALA   B CA  1 
ATOM   4312 C C   . ALA   B 1 209 ? -49.610 10.226  -1.420  1.00 56.51  ? 206 ALA   B C   1 
ATOM   4313 O O   . ALA   B 1 209 ? -48.635 10.186  -2.176  1.00 57.31  ? 206 ALA   B O   1 
ATOM   4314 C CB  . ALA   B 1 209 ? -49.288 9.360   0.920   1.00 45.09  ? 206 ALA   B CB  1 
ATOM   4315 N N   . VAL   B 1 210 ? -50.486 11.236  -1.403  1.00 58.12  ? 207 VAL   B N   1 
ATOM   4316 C CA  . VAL   B 1 210 ? -50.382 12.397  -2.287  1.00 50.20  ? 207 VAL   B CA  1 
ATOM   4317 C C   . VAL   B 1 210 ? -50.778 13.639  -1.496  1.00 50.77  ? 207 VAL   B C   1 
ATOM   4318 O O   . VAL   B 1 210 ? -51.945 13.792  -1.122  1.00 53.02  ? 207 VAL   B O   1 
ATOM   4319 C CB  . VAL   B 1 210 ? -51.261 12.273  -3.547  1.00 53.47  ? 207 VAL   B CB  1 
ATOM   4320 C CG1 . VAL   B 1 210 ? -51.093 13.509  -4.425  1.00 57.65  ? 207 VAL   B CG1 1 
ATOM   4321 C CG2 . VAL   B 1 210 ? -50.936 11.006  -4.345  1.00 51.87  ? 207 VAL   B CG2 1 
ATOM   4322 N N   . ILE   B 1 211 ? -49.818 14.529  -1.258  1.00 56.15  ? 208 ILE   B N   1 
ATOM   4323 C CA  . ILE   B 1 211 ? -50.050 15.799  -0.575  1.00 55.28  ? 208 ILE   B CA  1 
ATOM   4324 C C   . ILE   B 1 211 ? -50.649 16.812  -1.550  1.00 59.66  ? 208 ILE   B C   1 
ATOM   4325 O O   . ILE   B 1 211 ? -50.395 16.762  -2.759  1.00 58.92  ? 208 ILE   B O   1 
ATOM   4326 C CB  . ILE   B 1 211 ? -48.721 16.295  0.035   1.00 52.60  ? 208 ILE   B CB  1 
ATOM   4327 C CG1 . ILE   B 1 211 ? -48.281 15.332  1.142   1.00 59.71  ? 208 ILE   B CG1 1 
ATOM   4328 C CG2 . ILE   B 1 211 ? -48.843 17.697  0.596   1.00 55.89  ? 208 ILE   B CG2 1 
ATOM   4329 C CD1 . ILE   B 1 211 ? -46.879 15.536  1.654   1.00 59.69  ? 208 ILE   B CD1 1 
ATOM   4330 N N   . ASP   B 1 212 ? -51.481 17.725  -1.031  1.00 63.99  ? 209 ASP   B N   1 
ATOM   4331 C CA  . ASP   B 1 212 ? -51.973 18.866  -1.801  1.00 60.93  ? 209 ASP   B CA  1 
ATOM   4332 C C   . ASP   B 1 212 ? -51.040 20.038  -1.526  1.00 57.51  ? 209 ASP   B C   1 
ATOM   4333 O O   . ASP   B 1 212 ? -51.076 20.627  -0.440  1.00 52.45  ? 209 ASP   B O   1 
ATOM   4334 C CB  . ASP   B 1 212 ? -53.419 19.220  -1.442  1.00 63.99  ? 209 ASP   B CB  1 
ATOM   4335 C CG  . ASP   B 1 212 ? -54.138 20.016  -2.556  1.00 67.87  ? 209 ASP   B CG  1 
ATOM   4336 O OD1 . ASP   B 1 212 ? -53.571 21.006  -3.068  1.00 66.07  ? 209 ASP   B OD1 1 
ATOM   4337 O OD2 . ASP   B 1 212 ? -55.274 19.642  -2.933  1.00 71.47  ? 209 ASP   B OD2 1 
ATOM   4338 N N   . TYR   B 1 213 ? -50.201 20.374  -2.511  1.00 59.94  ? 210 TYR   B N   1 
ATOM   4339 C CA  . TYR   B 1 213 ? -49.236 21.448  -2.303  1.00 60.71  ? 210 TYR   B CA  1 
ATOM   4340 C C   . TYR   B 1 213 ? -49.919 22.805  -2.235  1.00 57.41  ? 210 TYR   B C   1 
ATOM   4341 O O   . TYR   B 1 213 ? -49.432 23.705  -1.541  1.00 55.71  ? 210 TYR   B O   1 
ATOM   4342 C CB  . TYR   B 1 213 ? -48.161 21.432  -3.396  1.00 54.04  ? 210 TYR   B CB  1 
ATOM   4343 C CG  . TYR   B 1 213 ? -48.629 21.763  -4.803  1.00 54.17  ? 210 TYR   B CG  1 
ATOM   4344 C CD1 . TYR   B 1 213 ? -48.733 23.085  -5.237  1.00 50.69  ? 210 TYR   B CD1 1 
ATOM   4345 C CD2 . TYR   B 1 213 ? -48.921 20.754  -5.712  1.00 52.01  ? 210 TYR   B CD2 1 
ATOM   4346 C CE1 . TYR   B 1 213 ? -49.153 23.391  -6.534  1.00 50.45  ? 210 TYR   B CE1 1 
ATOM   4347 C CE2 . TYR   B 1 213 ? -49.319 21.046  -7.013  1.00 52.80  ? 210 TYR   B CE2 1 
ATOM   4348 C CZ  . TYR   B 1 213 ? -49.443 22.369  -7.422  1.00 55.76  ? 210 TYR   B CZ  1 
ATOM   4349 O OH  . TYR   B 1 213 ? -49.851 22.661  -8.717  1.00 50.60  ? 210 TYR   B OH  1 
ATOM   4350 N N   . LYS   B 1 214 ? -51.036 22.970  -2.953  1.00 61.56  ? 211 LYS   B N   1 
ATOM   4351 C CA  . LYS   B 1 214 ? -51.805 24.209  -2.871  1.00 64.20  ? 211 LYS   B CA  1 
ATOM   4352 C C   . LYS   B 1 214 ? -52.367 24.404  -1.464  1.00 64.28  ? 211 LYS   B C   1 
ATOM   4353 O O   . LYS   B 1 214 ? -52.422 25.530  -0.952  1.00 61.89  ? 211 LYS   B O   1 
ATOM   4354 C CB  . LYS   B 1 214 ? -52.926 24.196  -3.919  1.00 58.32  ? 211 LYS   B CB  1 
ATOM   4355 C CG  . LYS   B 1 214 ? -52.460 23.940  -5.363  1.00 56.96  ? 211 LYS   B CG  1 
ATOM   4356 C CD  . LYS   B 1 214 ? -53.630 23.774  -6.347  1.00 57.92  ? 211 LYS   B CD  1 
ATOM   4357 C CE  . LYS   B 1 214 ? -53.155 23.791  -7.814  1.00 61.12  ? 211 LYS   B CE  1 
ATOM   4358 N NZ  . LYS   B 1 214 ? -54.236 23.581  -8.843  1.00 54.50  ? 211 LYS   B NZ  1 
ATOM   4359 N N   . LEU   B 1 215 ? -52.760 23.306  -0.812  1.00 62.89  ? 212 LEU   B N   1 
ATOM   4360 C CA  . LEU   B 1 215 ? -53.327 23.392  0.527   1.00 63.60  ? 212 LEU   B CA  1 
ATOM   4361 C C   . LEU   B 1 215 ? -52.249 23.627  1.575   1.00 65.71  ? 212 LEU   B C   1 
ATOM   4362 O O   . LEU   B 1 215 ? -52.448 24.411  2.513   1.00 61.72  ? 212 LEU   B O   1 
ATOM   4363 C CB  . LEU   B 1 215 ? -54.106 22.117  0.833   1.00 63.33  ? 212 LEU   B CB  1 
ATOM   4364 C CG  . LEU   B 1 215 ? -55.186 22.249  1.900   1.00 67.21  ? 212 LEU   B CG  1 
ATOM   4365 C CD1 . LEU   B 1 215 ? -55.777 23.665  1.922   1.00 67.67  ? 212 LEU   B CD1 1 
ATOM   4366 C CD2 . LEU   B 1 215 ? -56.262 21.215  1.629   1.00 65.26  ? 212 LEU   B CD2 1 
ATOM   4367 N N   . ALA   B 1 216 ? -51.102 22.964  1.418   1.00 66.10  ? 213 ALA   B N   1 
ATOM   4368 C CA  . ALA   B 1 216 ? -49.963 23.088  2.329   1.00 66.87  ? 213 ALA   B CA  1 
ATOM   4369 C C   . ALA   B 1 216 ? -49.075 24.240  1.854   1.00 71.96  ? 213 ALA   B C   1 
ATOM   4370 O O   . ALA   B 1 216 ? -48.152 24.060  1.056   1.00 74.08  ? 213 ALA   B O   1 
ATOM   4371 C CB  . ALA   B 1 216 ? -49.205 21.768  2.402   1.00 63.46  ? 213 ALA   B CB  1 
ATOM   4372 N N   . ASP   B 1 217 ? -49.359 25.440  2.370   1.00 70.86  ? 214 ASP   B N   1 
ATOM   4373 C CA  . ASP   B 1 217 ? -48.670 26.652  1.934   1.00 70.43  ? 214 ASP   B CA  1 
ATOM   4374 C C   . ASP   B 1 217 ? -47.168 26.565  2.156   1.00 70.73  ? 214 ASP   B C   1 
ATOM   4375 O O   . ASP   B 1 217 ? -46.375 26.620  1.208   1.00 66.70  ? 214 ASP   B O   1 
ATOM   4376 C CB  . ASP   B 1 217 ? -49.218 27.860  2.689   1.00 71.14  ? 214 ASP   B CB  1 
ATOM   4377 C CG  . ASP   B 1 217 ? -50.327 28.531  1.964   1.00 74.19  ? 214 ASP   B CG  1 
ATOM   4378 O OD1 . ASP   B 1 217 ? -51.090 27.813  1.288   1.00 69.69  ? 214 ASP   B OD1 1 
ATOM   4379 O OD2 . ASP   B 1 217 ? -50.422 29.775  2.056   1.00 81.44  ? 214 ASP   B OD2 1 
ATOM   4380 N N   . ASP   B 1 218 ? -46.761 26.466  3.416   1.00 72.62  ? 215 ASP   B N   1 
ATOM   4381 C CA  . ASP   B 1 218 ? -45.404 26.753  3.834   1.00 69.35  ? 215 ASP   B CA  1 
ATOM   4382 C C   . ASP   B 1 218 ? -44.696 25.480  4.277   1.00 65.61  ? 215 ASP   B C   1 
ATOM   4383 O O   . ASP   B 1 218 ? -45.230 24.366  4.164   1.00 63.91  ? 215 ASP   B O   1 
ATOM   4384 C CB  . ASP   B 1 218 ? -45.414 27.809  4.944   1.00 71.22  ? 215 ASP   B CB  1 
ATOM   4385 C CG  . ASP   B 1 218 ? -46.065 27.311  6.224   1.00 75.83  ? 215 ASP   B CG  1 
ATOM   4386 O OD1 . ASP   B 1 218 ? -47.023 26.503  6.151   1.00 70.60  ? 215 ASP   B OD1 1 
ATOM   4387 O OD2 . ASP   B 1 218 ? -45.613 27.737  7.310   1.00 77.61  ? 215 ASP   B OD2 1 
ATOM   4388 N N   . ALA   B 1 219 ? -43.469 25.660  4.774   1.00 67.24  ? 216 ALA   B N   1 
ATOM   4389 C CA  . ALA   B 1 219 ? -42.661 24.536  5.233   1.00 66.27  ? 216 ALA   B CA  1 
ATOM   4390 C C   . ALA   B 1 219 ? -43.374 23.755  6.331   1.00 70.61  ? 216 ALA   B C   1 
ATOM   4391 O O   . ALA   B 1 219 ? -43.442 22.520  6.281   1.00 65.19  ? 216 ALA   B O   1 
ATOM   4392 C CB  . ALA   B 1 219 ? -41.305 25.043  5.726   1.00 62.03  ? 216 ALA   B CB  1 
ATOM   4393 N N   . ASP   B 1 220 ? -43.930 24.465  7.318   1.00 70.12  ? 217 ASP   B N   1 
ATOM   4394 C CA  . ASP   B 1 220 ? -44.565 23.817  8.462   1.00 70.06  ? 217 ASP   B CA  1 
ATOM   4395 C C   . ASP   B 1 220 ? -45.689 22.883  8.023   1.00 67.31  ? 217 ASP   B C   1 
ATOM   4396 O O   . ASP   B 1 220 ? -45.615 21.668  8.240   1.00 66.57  ? 217 ASP   B O   1 
ATOM   4397 C CB  . ASP   B 1 220 ? -45.070 24.878  9.438   1.00 71.76  ? 217 ASP   B CB  1 
ATOM   4398 C CG  . ASP   B 1 220 ? -44.016 25.937  9.730   1.00 79.78  ? 217 ASP   B CG  1 
ATOM   4399 O OD1 . ASP   B 1 220 ? -43.651 26.688  8.795   1.00 84.74  ? 217 ASP   B OD1 1 
ATOM   4400 O OD2 . ASP   B 1 220 ? -43.535 26.015  10.881  1.00 78.74  ? 217 ASP   B OD2 1 
ATOM   4401 N N   . LYS   B 1 221 ? -46.707 23.391  7.362   1.00 62.75  ? 218 LYS   B N   1 
ATOM   4402 C CA  . LYS   B 1 221 ? -47.800 22.529  6.969   1.00 62.18  ? 218 LYS   B CA  1 
ATOM   4403 C C   . LYS   B 1 221 ? -47.307 21.359  6.155   1.00 63.55  ? 218 LYS   B C   1 
ATOM   4404 O O   . LYS   B 1 221 ? -47.868 20.276  6.200   1.00 61.49  ? 218 LYS   B O   1 
ATOM   4405 C CB  . LYS   B 1 221 ? -48.831 23.307  6.172   1.00 62.37  ? 218 LYS   B CB  1 
ATOM   4406 C CG  . LYS   B 1 221 ? -49.629 24.290  7.007   1.00 71.22  ? 218 LYS   B CG  1 
ATOM   4407 C CD  . LYS   B 1 221 ? -50.018 25.516  6.203   1.00 65.22  ? 218 LYS   B CD  1 
ATOM   4408 C CE  . LYS   B 1 221 ? -51.216 25.230  5.323   1.00 64.86  ? 218 LYS   B CE  1 
ATOM   4409 N NZ  . LYS   B 1 221 ? -51.508 26.366  4.412   1.00 69.82  ? 218 LYS   B NZ  1 
ATOM   4410 N N   . MET   B 1 222 ? -46.253 21.582  5.400   1.00 66.13  ? 219 MET   B N   1 
ATOM   4411 C CA  . MET   B 1 222 ? -45.707 20.525  4.558   1.00 64.15  ? 219 MET   B CA  1 
ATOM   4412 C C   . MET   B 1 222 ? -44.914 19.496  5.374   1.00 62.37  ? 219 MET   B C   1 
ATOM   4413 O O   . MET   B 1 222 ? -44.897 18.308  5.022   1.00 60.20  ? 219 MET   B O   1 
ATOM   4414 C CB  . MET   B 1 222 ? -44.864 21.165  3.441   1.00 60.77  ? 219 MET   B CB  1 
ATOM   4415 C CG  . MET   B 1 222 ? -44.419 20.214  2.333   1.00 56.66  ? 219 MET   B CG  1 
ATOM   4416 S SD  . MET   B 1 222 ? -45.751 19.349  1.453   1.00 70.25  ? 219 MET   B SD  1 
ATOM   4417 C CE  . MET   B 1 222 ? -46.392 20.707  0.488   1.00 63.21  ? 219 MET   B CE  1 
ATOM   4418 N N   . ARG   B 1 223 ? -44.383 19.897  6.503   1.00 56.59  ? 220 ARG   B N   1 
ATOM   4419 C CA  . ARG   B 1 223 ? -43.748 18.930  7.349   1.00 61.59  ? 220 ARG   B CA  1 
ATOM   4420 C C   . ARG   B 1 223 ? -44.818 18.041  7.952   1.00 62.17  ? 220 ARG   B C   1 
ATOM   4421 O O   . ARG   B 1 223 ? -44.659 16.834  8.005   1.00 56.50  ? 220 ARG   B O   1 
ATOM   4422 C CB  . ARG   B 1 223 ? -42.981 19.637  8.438   1.00 64.90  ? 220 ARG   B CB  1 
ATOM   4423 C CG  . ARG   B 1 223 ? -41.601 20.093  8.024   1.00 66.09  ? 220 ARG   B CG  1 
ATOM   4424 C CD  . ARG   B 1 223 ? -40.883 20.745  9.188   1.00 65.27  ? 220 ARG   B CD  1 
ATOM   4425 N NE  . ARG   B 1 223 ? -41.290 22.131  9.364   1.00 66.71  ? 220 ARG   B NE  1 
ATOM   4426 C CZ  . ARG   B 1 223 ? -40.703 23.157  8.761   1.00 73.02  ? 220 ARG   B CZ  1 
ATOM   4427 N NH1 . ARG   B 1 223 ? -39.682 22.950  7.944   1.00 63.07  ? 220 ARG   B NH1 1 
ATOM   4428 N NH2 . ARG   B 1 223 ? -41.137 24.388  8.978   1.00 73.19  ? 220 ARG   B NH2 1 
ATOM   4429 N N   . GLU   B 1 224 ? -45.924 18.632  8.386   1.00 62.18  ? 221 GLU   B N   1 
ATOM   4430 C CA  . GLU   B 1 224 ? -46.992 17.864  9.018   1.00 62.82  ? 221 GLU   B CA  1 
ATOM   4431 C C   . GLU   B 1 224 ? -47.540 16.806  8.071   1.00 59.48  ? 221 GLU   B C   1 
ATOM   4432 O O   . GLU   B 1 224 ? -47.728 15.647  8.460   1.00 60.56  ? 221 GLU   B O   1 
ATOM   4433 C CB  . GLU   B 1 224 ? -48.099 18.812  9.498   1.00 62.85  ? 221 GLU   B CB  1 
ATOM   4434 C CG  . GLU   B 1 224 ? -47.686 19.759  10.657  1.00 71.21  ? 221 GLU   B CG  1 
ATOM   4435 C CD  . GLU   B 1 224 ? -48.774 20.765  11.095  1.00 79.29  ? 221 GLU   B CD  1 
ATOM   4436 O OE1 . GLU   B 1 224 ? -49.814 20.903  10.409  1.00 77.15  ? 221 GLU   B OE1 1 
ATOM   4437 O OE2 . GLU   B 1 224 ? -48.589 21.441  12.130  1.00 80.01  ? 221 GLU   B OE2 1 
ATOM   4438 N N   . ALA   B 1 225 ? -47.775 17.183  6.811   1.00 57.80  ? 222 ALA   B N   1 
ATOM   4439 C CA  . ALA   B 1 225 ? -48.277 16.226  5.831   1.00 58.90  ? 222 ALA   B CA  1 
ATOM   4440 C C   . ALA   B 1 225 ? -47.232 15.159  5.509   1.00 61.49  ? 222 ALA   B C   1 
ATOM   4441 O O   . ALA   B 1 225 ? -47.565 13.977  5.346   1.00 60.11  ? 222 ALA   B O   1 
ATOM   4442 C CB  . ALA   B 1 225 ? -48.709 16.967  4.567   1.00 59.90  ? 222 ALA   B CB  1 
ATOM   4443 N N   . LEU   B 1 226 ? -45.962 15.559  5.424   1.00 60.31  ? 223 LEU   B N   1 
ATOM   4444 C CA  . LEU   B 1 226 ? -44.879 14.603  5.214   1.00 59.73  ? 223 LEU   B CA  1 
ATOM   4445 C C   . LEU   B 1 226 ? -44.681 13.682  6.420   1.00 59.94  ? 223 LEU   B C   1 
ATOM   4446 O O   . LEU   B 1 226 ? -44.491 12.468  6.251   1.00 55.95  ? 223 LEU   B O   1 
ATOM   4447 C CB  . LEU   B 1 226 ? -43.597 15.362  4.898   1.00 64.02  ? 223 LEU   B CB  1 
ATOM   4448 C CG  . LEU   B 1 226 ? -43.492 15.796  3.437   1.00 62.67  ? 223 LEU   B CG  1 
ATOM   4449 C CD1 . LEU   B 1 226 ? -42.354 16.783  3.263   1.00 56.22  ? 223 LEU   B CD1 1 
ATOM   4450 C CD2 . LEU   B 1 226 ? -43.286 14.560  2.586   1.00 45.33  ? 223 LEU   B CD2 1 
ATOM   4451 N N   . ARG   B 1 227 ? -44.688 14.244  7.642   1.00 62.31  ? 224 ARG   B N   1 
ATOM   4452 C CA  . ARG   B 1 227 ? -44.680 13.419  8.854   1.00 61.96  ? 224 ARG   B CA  1 
ATOM   4453 C C   . ARG   B 1 227 ? -45.758 12.343  8.795   1.00 62.47  ? 224 ARG   B C   1 
ATOM   4454 O O   . ARG   B 1 227 ? -45.508 11.178  9.130   1.00 62.63  ? 224 ARG   B O   1 
ATOM   4455 C CB  . ARG   B 1 227 ? -44.895 14.284  10.096  1.00 60.06  ? 224 ARG   B CB  1 
ATOM   4456 C CG  . ARG   B 1 227 ? -43.741 15.178  10.483  1.00 61.47  ? 224 ARG   B CG  1 
ATOM   4457 C CD  . ARG   B 1 227 ? -44.043 15.861  11.808  1.00 70.42  ? 224 ARG   B CD  1 
ATOM   4458 N NE  . ARG   B 1 227 ? -43.791 17.298  11.778  1.00 69.61  ? 224 ARG   B NE  1 
ATOM   4459 C CZ  . ARG   B 1 227 ? -42.592 17.850  11.927  1.00 75.41  ? 224 ARG   B CZ  1 
ATOM   4460 N NH1 . ARG   B 1 227 ? -41.504 17.107  12.078  1.00 71.45  ? 224 ARG   B NH1 1 
ATOM   4461 N NH2 . ARG   B 1 227 ? -42.482 19.179  11.923  1.00 71.45  ? 224 ARG   B NH2 1 
ATOM   4462 N N   . GLU   B 1 228 ? -46.963 12.720  8.359   1.00 56.86  ? 225 GLU   B N   1 
ATOM   4463 C CA  . GLU   B 1 228 ? -48.029 11.750  8.157   1.00 55.61  ? 225 GLU   B CA  1 
ATOM   4464 C C   . GLU   B 1 228 ? -47.713 10.819  6.990   1.00 60.65  ? 225 GLU   B C   1 
ATOM   4465 O O   . GLU   B 1 228 ? -47.805 9.593   7.116   1.00 60.83  ? 225 GLU   B O   1 
ATOM   4466 C CB  . GLU   B 1 228 ? -49.348 12.494  7.923   1.00 62.63  ? 225 GLU   B CB  1 
ATOM   4467 C CG  . GLU   B 1 228 ? -50.620 11.691  8.213   1.00 69.74  ? 225 GLU   B CG  1 
ATOM   4468 C CD  . GLU   B 1 228 ? -51.267 11.091  6.969   1.00 66.71  ? 225 GLU   B CD  1 
ATOM   4469 O OE1 . GLU   B 1 228 ? -50.562 10.902  5.958   1.00 71.90  ? 225 GLU   B OE1 1 
ATOM   4470 O OE2 . GLU   B 1 228 ? -52.491 10.815  7.005   1.00 68.21  ? 225 GLU   B OE2 1 
ATOM   4471 N N   . ALA   B 1 229 ? -47.333 11.384  5.843   1.00 62.59  ? 226 ALA   B N   1 
ATOM   4472 C CA  . ALA   B 1 229 ? -47.196 10.587  4.627   1.00 58.79  ? 226 ALA   B CA  1 
ATOM   4473 C C   . ALA   B 1 229 ? -45.958 9.696   4.634   1.00 59.41  ? 226 ALA   B C   1 
ATOM   4474 O O   . ALA   B 1 229 ? -45.955 8.646   3.976   1.00 50.78  ? 226 ALA   B O   1 
ATOM   4475 C CB  . ALA   B 1 229 ? -47.158 11.508  3.408   1.00 62.26  ? 226 ALA   B CB  1 
ATOM   4476 N N   . ALA   B 1 230 ? -44.899 10.106  5.337   1.00 60.94  ? 227 ALA   B N   1 
ATOM   4477 C CA  . ALA   B 1 230 ? -43.654 9.343   5.418   1.00 61.43  ? 227 ALA   B CA  1 
ATOM   4478 C C   . ALA   B 1 230 ? -43.178 9.375   6.864   1.00 64.70  ? 227 ALA   B C   1 
ATOM   4479 O O   . ALA   B 1 230 ? -42.385 10.242  7.260   1.00 62.13  ? 227 ALA   B O   1 
ATOM   4480 C CB  . ALA   B 1 230 ? -42.593 9.899   4.466   1.00 59.43  ? 227 ALA   B CB  1 
ATOM   4481 N N   . PRO   B 1 231 ? -43.665 8.443   7.695   1.00 67.27  ? 228 PRO   B N   1 
ATOM   4482 C CA  . PRO   B 1 231 ? -43.313 8.462   9.129   1.00 67.07  ? 228 PRO   B CA  1 
ATOM   4483 C C   . PRO   B 1 231 ? -41.947 7.880   9.460   1.00 60.32  ? 228 PRO   B C   1 
ATOM   4484 O O   . PRO   B 1 231 ? -41.389 8.223   10.510  1.00 58.85  ? 228 PRO   B O   1 
ATOM   4485 C CB  . PRO   B 1 231 ? -44.428 7.627   9.767   1.00 61.37  ? 228 PRO   B CB  1 
ATOM   4486 C CG  . PRO   B 1 231 ? -44.845 6.688   8.675   1.00 60.40  ? 228 PRO   B CG  1 
ATOM   4487 C CD  . PRO   B 1 231 ? -44.696 7.437   7.383   1.00 57.55  ? 228 PRO   B CD  1 
ATOM   4488 N N   . ASP   B 1 232 ? -41.395 7.023   8.606   1.00 64.15  ? 229 ASP   B N   1 
ATOM   4489 C CA  . ASP   B 1 232 ? -40.054 6.471   8.761   1.00 64.00  ? 229 ASP   B CA  1 
ATOM   4490 C C   . ASP   B 1 232 ? -38.950 7.361   8.171   1.00 64.51  ? 229 ASP   B C   1 
ATOM   4491 O O   . ASP   B 1 232 ? -37.816 6.888   8.007   1.00 60.50  ? 229 ASP   B O   1 
ATOM   4492 C CB  . ASP   B 1 232 ? -39.984 5.085   8.109   1.00 63.89  ? 229 ASP   B CB  1 
ATOM   4493 C CG  . ASP   B 1 232 ? -40.802 4.044   8.851   1.00 71.14  ? 229 ASP   B CG  1 
ATOM   4494 O OD1 . ASP   B 1 232 ? -40.599 3.894   10.078  1.00 76.99  ? 229 ASP   B OD1 1 
ATOM   4495 O OD2 . ASP   B 1 232 ? -41.649 3.378   8.208   1.00 69.02  ? 229 ASP   B OD2 1 
ATOM   4496 N N   . GLY   B 1 233 ? -39.253 8.622   7.839   1.00 61.35  ? 230 GLY   B N   1 
ATOM   4497 C CA  . GLY   B 1 233 ? -38.293 9.508   7.211   1.00 52.25  ? 230 GLY   B CA  1 
ATOM   4498 C C   . GLY   B 1 233 ? -38.160 9.276   5.713   1.00 54.63  ? 230 GLY   B C   1 
ATOM   4499 O O   . GLY   B 1 233 ? -38.687 8.319   5.141   1.00 55.27  ? 230 GLY   B O   1 
ATOM   4500 N N   . VAL   B 1 234 ? -37.419 10.179  5.064   1.00 54.85  ? 231 VAL   B N   1 
ATOM   4501 C CA  . VAL   B 1 234 ? -37.226 10.163  3.614   1.00 46.56  ? 231 VAL   B CA  1 
ATOM   4502 C C   . VAL   B 1 234 ? -35.887 9.518   3.301   1.00 45.02  ? 231 VAL   B C   1 
ATOM   4503 O O   . VAL   B 1 234 ? -34.840 9.996   3.757   1.00 44.47  ? 231 VAL   B O   1 
ATOM   4504 C CB  . VAL   B 1 234 ? -37.275 11.580  3.022   1.00 48.39  ? 231 VAL   B CB  1 
ATOM   4505 C CG1 . VAL   B 1 234 ? -37.164 11.531  1.487   1.00 42.32  ? 231 VAL   B CG1 1 
ATOM   4506 C CG2 . VAL   B 1 234 ? -38.522 12.308  3.465   1.00 47.62  ? 231 VAL   B CG2 1 
ATOM   4507 N N   . ASP   B 1 235 ? -35.912 8.466   2.482   1.00 46.26  ? 232 ASP   B N   1 
ATOM   4508 C CA  . ASP   B 1 235 ? -34.698 7.839   1.969   1.00 43.80  ? 232 ASP   B CA  1 
ATOM   4509 C C   . ASP   B 1 235 ? -34.282 8.356   0.597   1.00 49.07  ? 232 ASP   B C   1 
ATOM   4510 O O   . ASP   B 1 235 ? -33.082 8.444   0.316   1.00 41.50  ? 232 ASP   B O   1 
ATOM   4511 C CB  . ASP   B 1 235 ? -34.881 6.328   1.882   1.00 42.07  ? 232 ASP   B CB  1 
ATOM   4512 C CG  . ASP   B 1 235 ? -35.404 5.736   3.158   1.00 53.38  ? 232 ASP   B CG  1 
ATOM   4513 O OD1 . ASP   B 1 235 ? -34.835 6.046   4.246   1.00 48.50  ? 232 ASP   B OD1 1 
ATOM   4514 O OD2 . ASP   B 1 235 ? -36.394 4.967   3.064   1.00 55.20  ? 232 ASP   B OD2 1 
ATOM   4515 N N   . LYS   B 1 236 ? -35.243 8.631   -0.291  1.00 45.47  ? 233 LYS   B N   1 
ATOM   4516 C CA  . LYS   B 1 236 ? -34.966 9.275   -1.562  1.00 42.77  ? 233 LYS   B CA  1 
ATOM   4517 C C   . LYS   B 1 236 ? -35.939 10.428  -1.747  1.00 45.31  ? 233 LYS   B C   1 
ATOM   4518 O O   . LYS   B 1 236 ? -37.090 10.363  -1.305  1.00 42.56  ? 233 LYS   B O   1 
ATOM   4519 C CB  . LYS   B 1 236 ? -35.072 8.322   -2.757  1.00 38.44  ? 233 LYS   B CB  1 
ATOM   4520 C CG  . LYS   B 1 236 ? -34.707 6.888   -2.465  1.00 43.77  ? 233 LYS   B CG  1 
ATOM   4521 C CD  . LYS   B 1 236 ? -33.228 6.600   -2.573  1.00 42.36  ? 233 LYS   B CD  1 
ATOM   4522 C CE  . LYS   B 1 236 ? -33.038 5.099   -2.588  1.00 44.83  ? 233 LYS   B CE  1 
ATOM   4523 N NZ  . LYS   B 1 236 ? -31.841 4.603   -1.868  1.00 47.70  ? 233 LYS   B NZ  1 
ATOM   4524 N N   . TYR   B 1 237 ? -35.451 11.484  -2.405  1.00 37.57  ? 234 TYR   B N   1 
ATOM   4525 C CA  . TYR   B 1 237 ? -36.239 12.653  -2.772  1.00 35.60  ? 234 TYR   B CA  1 
ATOM   4526 C C   . TYR   B 1 237 ? -35.914 13.045  -4.209  1.00 44.41  ? 234 TYR   B C   1 
ATOM   4527 O O   . TYR   B 1 237 ? -34.766 13.375  -4.524  1.00 44.79  ? 234 TYR   B O   1 
ATOM   4528 C CB  . TYR   B 1 237 ? -35.940 13.812  -1.841  1.00 33.91  ? 234 TYR   B CB  1 
ATOM   4529 C CG  . TYR   B 1 237 ? -36.770 15.042  -2.081  1.00 39.77  ? 234 TYR   B CG  1 
ATOM   4530 C CD1 . TYR   B 1 237 ? -38.022 14.968  -2.704  1.00 41.98  ? 234 TYR   B CD1 1 
ATOM   4531 C CD2 . TYR   B 1 237 ? -36.307 16.285  -1.680  1.00 36.33  ? 234 TYR   B CD2 1 
ATOM   4532 C CE1 . TYR   B 1 237 ? -38.783 16.108  -2.909  1.00 38.36  ? 234 TYR   B CE1 1 
ATOM   4533 C CE2 . TYR   B 1 237 ? -37.045 17.414  -1.883  1.00 40.93  ? 234 TYR   B CE2 1 
ATOM   4534 C CZ  . TYR   B 1 237 ? -38.281 17.329  -2.496  1.00 40.76  ? 234 TYR   B CZ  1 
ATOM   4535 O OH  . TYR   B 1 237 ? -38.989 18.495  -2.670  1.00 44.92  ? 234 TYR   B OH  1 
ATOM   4536 N N   . PHE   B 1 238 ? -36.917 13.024  -5.075  1.00 43.57  ? 235 PHE   B N   1 
ATOM   4537 C CA  . PHE   B 1 238 ? -36.782 13.511  -6.445  1.00 40.55  ? 235 PHE   B CA  1 
ATOM   4538 C C   . PHE   B 1 238 ? -37.452 14.878  -6.494  1.00 41.71  ? 235 PHE   B C   1 
ATOM   4539 O O   . PHE   B 1 238 ? -38.678 14.975  -6.548  1.00 45.92  ? 235 PHE   B O   1 
ATOM   4540 C CB  . PHE   B 1 238 ? -37.405 12.535  -7.430  1.00 38.81  ? 235 PHE   B CB  1 
ATOM   4541 C CG  . PHE   B 1 238 ? -37.142 12.872  -8.858  1.00 36.32  ? 235 PHE   B CG  1 
ATOM   4542 C CD1 . PHE   B 1 238 ? -37.896 13.833  -9.503  1.00 34.32  ? 235 PHE   B CD1 1 
ATOM   4543 C CD2 . PHE   B 1 238 ? -36.151 12.215  -9.563  1.00 36.64  ? 235 PHE   B CD2 1 
ATOM   4544 C CE1 . PHE   B 1 238 ? -37.656 14.146  -10.821 1.00 33.44  ? 235 PHE   B CE1 1 
ATOM   4545 C CE2 . PHE   B 1 238 ? -35.906 12.519  -10.893 1.00 37.29  ? 235 PHE   B CE2 1 
ATOM   4546 C CZ  . PHE   B 1 238 ? -36.666 13.492  -11.517 1.00 38.11  ? 235 PHE   B CZ  1 
ATOM   4547 N N   . ASP   B 1 239 ? -36.642 15.930  -6.471  1.00 39.36  ? 236 ASP   B N   1 
ATOM   4548 C CA  . ASP   B 1 239 ? -37.123 17.300  -6.369  1.00 39.83  ? 236 ASP   B CA  1 
ATOM   4549 C C   . ASP   B 1 239 ? -37.265 17.941  -7.750  1.00 46.08  ? 236 ASP   B C   1 
ATOM   4550 O O   . ASP   B 1 239 ? -36.314 17.938  -8.544  1.00 38.74  ? 236 ASP   B O   1 
ATOM   4551 C CB  . ASP   B 1 239 ? -36.163 18.121  -5.515  1.00 33.39  ? 236 ASP   B CB  1 
ATOM   4552 C CG  . ASP   B 1 239 ? -36.768 19.414  -5.054  1.00 37.20  ? 236 ASP   B CG  1 
ATOM   4553 O OD1 . ASP   B 1 239 ? -37.950 19.655  -5.382  1.00 39.31  ? 236 ASP   B OD1 1 
ATOM   4554 O OD2 . ASP   B 1 239 ? -36.071 20.187  -4.350  1.00 34.74  ? 236 ASP   B OD2 1 
ATOM   4555 N N   . SER   B 1 240 ? -38.460 18.493  -8.028  1.00 40.22  ? 237 SER   B N   1 
ATOM   4556 C CA  . SER   B 1 240 ? -38.700 19.334  -9.194  1.00 36.58  ? 237 SER   B CA  1 
ATOM   4557 C C   . SER   B 1 240 ? -39.231 20.706  -8.814  1.00 38.12  ? 237 SER   B C   1 
ATOM   4558 O O   . SER   B 1 240 ? -39.427 21.546  -9.701  1.00 39.21  ? 237 SER   B O   1 
ATOM   4559 C CB  . SER   B 1 240 ? -39.688 18.670  -10.169 1.00 38.13  ? 237 SER   B CB  1 
ATOM   4560 O OG  . SER   B 1 240 ? -39.063 17.690  -10.979 1.00 42.15  ? 237 SER   B OG  1 
ATOM   4561 N N   . ILE   B 1 241 ? -39.444 20.963  -7.523  1.00 32.31  ? 238 ILE   B N   1 
ATOM   4562 C CA  . ILE   B 1 241 ? -40.199 22.115  -7.061  1.00 33.01  ? 238 ILE   B CA  1 
ATOM   4563 C C   . ILE   B 1 241 ? -39.352 23.054  -6.215  1.00 35.49  ? 238 ILE   B C   1 
ATOM   4564 O O   . ILE   B 1 241 ? -39.462 24.281  -6.346  1.00 36.04  ? 238 ILE   B O   1 
ATOM   4565 C CB  . ILE   B 1 241 ? -41.452 21.664  -6.272  1.00 38.57  ? 238 ILE   B CB  1 
ATOM   4566 C CG1 . ILE   B 1 241 ? -42.392 20.861  -7.175  1.00 37.47  ? 238 ILE   B CG1 1 
ATOM   4567 C CG2 . ILE   B 1 241 ? -42.156 22.854  -5.634  1.00 31.34  ? 238 ILE   B CG2 1 
ATOM   4568 C CD1 . ILE   B 1 241 ? -42.775 21.597  -8.455  1.00 40.29  ? 238 ILE   B CD1 1 
ATOM   4569 N N   . GLY   B 1 242 ? -38.518 22.505  -5.328  1.00 38.41  ? 239 GLY   B N   1 
ATOM   4570 C CA  . GLY   B 1 242 ? -37.737 23.294  -4.392  1.00 35.94  ? 239 GLY   B CA  1 
ATOM   4571 C C   . GLY   B 1 242 ? -38.655 24.074  -3.471  1.00 41.15  ? 239 GLY   B C   1 
ATOM   4572 O O   . GLY   B 1 242 ? -39.799 23.686  -3.207  1.00 41.74  ? 239 GLY   B O   1 
ATOM   4573 N N   . GLY   B 1 243 ? -38.165 25.208  -2.992  1.00 39.81  ? 240 GLY   B N   1 
ATOM   4574 C CA  . GLY   B 1 243 ? -39.014 25.994  -2.124  1.00 41.19  ? 240 GLY   B CA  1 
ATOM   4575 C C   . GLY   B 1 243 ? -39.337 25.245  -0.845  1.00 47.35  ? 240 GLY   B C   1 
ATOM   4576 O O   . GLY   B 1 243 ? -38.524 24.477  -0.314  1.00 44.73  ? 240 GLY   B O   1 
ATOM   4577 N N   . SER   B 1 244 ? -40.564 25.449  -0.359  1.00 48.81  ? 241 SER   B N   1 
ATOM   4578 C CA  . SER   B 1 244 ? -40.915 25.064  1.004   1.00 48.83  ? 241 SER   B CA  1 
ATOM   4579 C C   . SER   B 1 244 ? -41.136 23.562  1.143   1.00 47.81  ? 241 SER   B C   1 
ATOM   4580 O O   . SER   B 1 244 ? -40.888 23.011  2.221   1.00 46.13  ? 241 SER   B O   1 
ATOM   4581 C CB  . SER   B 1 244 ? -42.153 25.840  1.468   1.00 46.32  ? 241 SER   B CB  1 
ATOM   4582 O OG  . SER   B 1 244 ? -43.323 25.382  0.810   1.00 51.20  ? 241 SER   B OG  1 
ATOM   4583 N N   . VAL   B 1 245 ? -41.582 22.881  0.081   1.00 43.45  ? 242 VAL   B N   1 
ATOM   4584 C CA  . VAL   B 1 245 ? -41.669 21.423  0.138   1.00 43.55  ? 242 VAL   B CA  1 
ATOM   4585 C C   . VAL   B 1 245 ? -40.283 20.822  0.344   1.00 46.47  ? 242 VAL   B C   1 
ATOM   4586 O O   . VAL   B 1 245 ? -40.097 19.925  1.177   1.00 44.59  ? 242 VAL   B O   1 
ATOM   4587 C CB  . VAL   B 1 245 ? -42.355 20.860  -1.126  1.00 44.85  ? 242 VAL   B CB  1 
ATOM   4588 C CG1 . VAL   B 1 245 ? -41.641 21.294  -2.390  1.00 43.04  ? 242 VAL   B CG1 1 
ATOM   4589 C CG2 . VAL   B 1 245 ? -42.428 19.328  -1.069  1.00 42.03  ? 242 VAL   B CG2 1 
ATOM   4590 N N   . THR   B 1 246 ? -39.285 21.332  -0.393  1.00 47.57  ? 243 THR   B N   1 
ATOM   4591 C CA  . THR   B 1 246 ? -37.914 20.847  -0.278  1.00 46.60  ? 243 THR   B CA  1 
ATOM   4592 C C   . THR   B 1 246 ? -37.318 21.192  1.076   1.00 45.81  ? 243 THR   B C   1 
ATOM   4593 O O   . THR   B 1 246 ? -36.559 20.396  1.647   1.00 46.31  ? 243 THR   B O   1 
ATOM   4594 C CB  . THR   B 1 246 ? -37.058 21.427  -1.409  1.00 44.78  ? 243 THR   B CB  1 
ATOM   4595 O OG1 . THR   B 1 246 ? -37.401 20.778  -2.641  1.00 37.89  ? 243 THR   B OG1 1 
ATOM   4596 C CG2 . THR   B 1 246 ? -35.562 21.244  -1.133  1.00 37.88  ? 243 THR   B CG2 1 
ATOM   4597 N N   . ASP   B 1 247 ? -37.642 22.371  1.607   1.00 42.82  ? 244 ASP   B N   1 
ATOM   4598 C CA  . ASP   B 1 247 ? -37.206 22.696  2.960   1.00 46.16  ? 244 ASP   B CA  1 
ATOM   4599 C C   . ASP   B 1 247 ? -37.742 21.678  3.961   1.00 49.74  ? 244 ASP   B C   1 
ATOM   4600 O O   . ASP   B 1 247 ? -37.007 21.193  4.831   1.00 51.17  ? 244 ASP   B O   1 
ATOM   4601 C CB  . ASP   B 1 247 ? -37.657 24.107  3.336   1.00 52.76  ? 244 ASP   B CB  1 
ATOM   4602 C CG  . ASP   B 1 247 ? -36.910 25.199  2.567   1.00 55.72  ? 244 ASP   B CG  1 
ATOM   4603 O OD1 . ASP   B 1 247 ? -35.723 24.998  2.218   1.00 60.72  ? 244 ASP   B OD1 1 
ATOM   4604 O OD2 . ASP   B 1 247 ? -37.509 26.274  2.332   1.00 54.29  ? 244 ASP   B OD2 1 
ATOM   4605 N N   . ALA   B 1 248 ? -39.020 21.326  3.839   1.00 45.84  ? 245 ALA   B N   1 
ATOM   4606 C CA  . ALA   B 1 248 ? -39.595 20.316  4.716   1.00 50.04  ? 245 ALA   B CA  1 
ATOM   4607 C C   . ALA   B 1 248 ? -38.822 19.007  4.631   1.00 49.72  ? 245 ALA   B C   1 
ATOM   4608 O O   . ALA   B 1 248 ? -38.402 18.455  5.654   1.00 50.54  ? 245 ALA   B O   1 
ATOM   4609 C CB  . ALA   B 1 248 ? -41.070 20.101  4.363   1.00 50.49  ? 245 ALA   B CB  1 
ATOM   4610 N N   . VAL   B 1 249 ? -38.611 18.504  3.413   1.00 44.93  ? 246 VAL   B N   1 
ATOM   4611 C CA  . VAL   B 1 249 ? -38.013 17.184  3.248   1.00 45.02  ? 246 VAL   B CA  1 
ATOM   4612 C C   . VAL   B 1 249 ? -36.637 17.127  3.900   1.00 47.05  ? 246 VAL   B C   1 
ATOM   4613 O O   . VAL   B 1 249 ? -36.259 16.114  4.501   1.00 49.53  ? 246 VAL   B O   1 
ATOM   4614 C CB  . VAL   B 1 249 ? -37.951 16.802  1.758   1.00 46.07  ? 246 VAL   B CB  1 
ATOM   4615 C CG1 . VAL   B 1 249 ? -37.194 15.486  1.568   1.00 46.16  ? 246 VAL   B CG1 1 
ATOM   4616 C CG2 . VAL   B 1 249 ? -39.368 16.694  1.173   1.00 42.39  ? 246 VAL   B CG2 1 
ATOM   4617 N N   . PHE   B 1 250 ? -35.877 18.215  3.817   1.00 50.05  ? 247 PHE   B N   1 
ATOM   4618 C CA  . PHE   B 1 250 ? -34.510 18.193  4.323   1.00 48.75  ? 247 PHE   B CA  1 
ATOM   4619 C C   . PHE   B 1 250 ? -34.458 18.082  5.840   1.00 47.39  ? 247 PHE   B C   1 
ATOM   4620 O O   . PHE   B 1 250 ? -33.445 17.623  6.382   1.00 52.72  ? 247 PHE   B O   1 
ATOM   4621 C CB  . PHE   B 1 250 ? -33.750 19.434  3.829   1.00 46.02  ? 247 PHE   B CB  1 
ATOM   4622 C CG  . PHE   B 1 250 ? -33.013 19.212  2.532   1.00 41.43  ? 247 PHE   B CG  1 
ATOM   4623 C CD1 . PHE   B 1 250 ? -33.704 18.864  1.373   1.00 41.28  ? 247 PHE   B CD1 1 
ATOM   4624 C CD2 . PHE   B 1 250 ? -31.624 19.338  2.470   1.00 40.63  ? 247 PHE   B CD2 1 
ATOM   4625 C CE1 . PHE   B 1 250 ? -33.019 18.643  0.159   1.00 40.45  ? 247 PHE   B CE1 1 
ATOM   4626 C CE2 . PHE   B 1 250 ? -30.931 19.125  1.264   1.00 39.33  ? 247 PHE   B CE2 1 
ATOM   4627 C CZ  . PHE   B 1 250 ? -31.628 18.778  0.108   1.00 34.56  ? 247 PHE   B CZ  1 
ATOM   4628 N N   . SER   B 1 251 ? -35.536 18.454  6.533   1.00 49.07  ? 248 SER   B N   1 
ATOM   4629 C CA  . SER   B 1 251 ? -35.613 18.320  7.989   1.00 46.71  ? 248 SER   B CA  1 
ATOM   4630 C C   . SER   B 1 251 ? -35.784 16.878  8.456   1.00 41.33  ? 248 SER   B C   1 
ATOM   4631 O O   . SER   B 1 251 ? -35.687 16.631  9.663   1.00 48.08  ? 248 SER   B O   1 
ATOM   4632 C CB  . SER   B 1 251 ? -36.778 19.148  8.528   1.00 40.86  ? 248 SER   B CB  1 
ATOM   4633 O OG  . SER   B 1 251 ? -38.005 18.524  8.183   1.00 44.98  ? 248 SER   B OG  1 
ATOM   4634 N N   . MET   B 1 252 ? -36.022 15.933  7.540   1.00 37.03  ? 249 MET   B N   1 
ATOM   4635 C CA  . MET   B 1 252 ? -36.393 14.560  7.867   1.00 36.41  ? 249 MET   B CA  1 
ATOM   4636 C C   . MET   B 1 252 ? -35.700 13.559  6.957   1.00 44.90  ? 249 MET   B C   1 
ATOM   4637 O O   . MET   B 1 252 ? -36.271 12.509  6.626   1.00 40.25  ? 249 MET   B O   1 
ATOM   4638 C CB  . MET   B 1 252 ? -37.901 14.361  7.774   1.00 43.46  ? 249 MET   B CB  1 
ATOM   4639 C CG  . MET   B 1 252 ? -38.579 15.348  6.842   1.00 54.13  ? 249 MET   B CG  1 
ATOM   4640 S SD  . MET   B 1 252 ? -40.382 15.224  6.807   1.00 60.15  ? 249 MET   B SD  1 
ATOM   4641 C CE  . MET   B 1 252 ? -40.574 13.769  5.781   1.00 48.25  ? 249 MET   B CE  1 
ATOM   4642 N N   . LEU   B 1 253 ? -34.471 13.873  6.542   1.00 46.74  ? 250 LEU   B N   1 
ATOM   4643 C CA  . LEU   B 1 253 ? -33.678 12.977  5.706   1.00 43.42  ? 250 LEU   B CA  1 
ATOM   4644 C C   . LEU   B 1 253 ? -33.107 11.854  6.566   1.00 41.89  ? 250 LEU   B C   1 
ATOM   4645 O O   . LEU   B 1 253 ? -32.599 12.098  7.663   1.00 37.55  ? 250 LEU   B O   1 
ATOM   4646 C CB  . LEU   B 1 253 ? -32.552 13.754  5.006   1.00 42.53  ? 250 LEU   B CB  1 
ATOM   4647 C CG  . LEU   B 1 253 ? -32.944 14.670  3.828   1.00 43.25  ? 250 LEU   B CG  1 
ATOM   4648 C CD1 . LEU   B 1 253 ? -31.871 15.695  3.451   1.00 40.36  ? 250 LEU   B CD1 1 
ATOM   4649 C CD2 . LEU   B 1 253 ? -33.273 13.810  2.620   1.00 38.48  ? 250 LEU   B CD2 1 
ATOM   4650 N N   . ASN   B 1 254 ? -33.199 10.627  6.071   1.00 42.36  ? 251 ASN   B N   1 
ATOM   4651 C CA  . ASN   B 1 254 ? -32.639 9.484   6.767   1.00 42.10  ? 251 ASN   B CA  1 
ATOM   4652 C C   . ASN   B 1 254 ? -31.155 9.328   6.451   1.00 45.26  ? 251 ASN   B C   1 
ATOM   4653 O O   . ASN   B 1 254 ? -30.611 9.930   5.522   1.00 44.40  ? 251 ASN   B O   1 
ATOM   4654 C CB  . ASN   B 1 254 ? -33.365 8.197   6.378   1.00 41.25  ? 251 ASN   B CB  1 
ATOM   4655 C CG  . ASN   B 1 254 ? -34.796 8.181   6.834   1.00 45.87  ? 251 ASN   B CG  1 
ATOM   4656 O OD1 . ASN   B 1 254 ? -35.186 8.911   7.749   1.00 41.39  ? 251 ASN   B OD1 1 
ATOM   4657 N ND2 . ASN   B 1 254 ? -35.596 7.340   6.199   1.00 49.09  ? 251 ASN   B ND2 1 
ATOM   4658 N N   . VAL   B 1 255 ? -30.504 8.469   7.234   1.00 45.13  ? 252 VAL   B N   1 
ATOM   4659 C CA  . VAL   B 1 255 ? -29.099 8.184   7.009   1.00 43.13  ? 252 VAL   B CA  1 
ATOM   4660 C C   . VAL   B 1 255 ? -28.926 7.533   5.648   1.00 39.33  ? 252 VAL   B C   1 
ATOM   4661 O O   . VAL   B 1 255 ? -29.603 6.554   5.324   1.00 43.52  ? 252 VAL   B O   1 
ATOM   4662 C CB  . VAL   B 1 255 ? -28.556 7.291   8.133   1.00 38.52  ? 252 VAL   B CB  1 
ATOM   4663 C CG1 . VAL   B 1 255 ? -27.245 6.636   7.695   1.00 27.39  ? 252 VAL   B CG1 1 
ATOM   4664 C CG2 . VAL   B 1 255 ? -28.401 8.115   9.424   1.00 29.40  ? 252 VAL   B CG2 1 
ATOM   4665 N N   . GLY   B 1 256 ? -28.000 8.064   4.851   1.00 37.00  ? 253 GLY   B N   1 
ATOM   4666 C CA  . GLY   B 1 256 ? -27.699 7.508   3.551   1.00 38.34  ? 253 GLY   B CA  1 
ATOM   4667 C C   . GLY   B 1 256 ? -28.643 7.929   2.451   1.00 38.55  ? 253 GLY   B C   1 
ATOM   4668 O O   . GLY   B 1 256 ? -28.615 7.333   1.363   1.00 31.53  ? 253 GLY   B O   1 
ATOM   4669 N N   . SER   B 1 257 ? -29.472 8.940   2.706   1.00 39.20  ? 254 SER   B N   1 
ATOM   4670 C CA  . SER   B 1 257 ? -30.506 9.362   1.778   1.00 37.94  ? 254 SER   B CA  1 
ATOM   4671 C C   . SER   B 1 257 ? -29.901 9.949   0.507   1.00 39.58  ? 254 SER   B C   1 
ATOM   4672 O O   . SER   B 1 257 ? -28.754 10.411  0.481   1.00 43.61  ? 254 SER   B O   1 
ATOM   4673 C CB  . SER   B 1 257 ? -31.427 10.378  2.448   1.00 37.95  ? 254 SER   B CB  1 
ATOM   4674 O OG  . SER   B 1 257 ? -30.698 11.470  2.952   1.00 35.82  ? 254 SER   B OG  1 
ATOM   4675 N N   . GLN   B 1 258 ? -30.692 9.908   -0.564  1.00 37.70  ? 255 GLN   B N   1 
ATOM   4676 C CA  . GLN   B 1 258 ? -30.318 10.453  -1.863  1.00 38.02  ? 255 GLN   B CA  1 
ATOM   4677 C C   . GLN   B 1 258 ? -31.365 11.457  -2.299  1.00 38.65  ? 255 GLN   B C   1 
ATOM   4678 O O   . GLN   B 1 258 ? -32.555 11.139  -2.313  1.00 39.12  ? 255 GLN   B O   1 
ATOM   4679 C CB  . GLN   B 1 258 ? -30.200 9.358   -2.916  1.00 38.03  ? 255 GLN   B CB  1 
ATOM   4680 C CG  . GLN   B 1 258 ? -29.022 8.460   -2.730  1.00 33.90  ? 255 GLN   B CG  1 
ATOM   4681 C CD  . GLN   B 1 258 ? -29.039 7.337   -3.711  1.00 37.36  ? 255 GLN   B CD  1 
ATOM   4682 O OE1 . GLN   B 1 258 ? -30.056 6.676   -3.900  1.00 43.99  ? 255 GLN   B OE1 1 
ATOM   4683 N NE2 . GLN   B 1 258 ? -27.916 7.114   -4.359  1.00 38.51  ? 255 GLN   B NE2 1 
ATOM   4684 N N   . VAL   B 1 259 ? -30.916 12.661  -2.648  1.00 36.65  ? 256 VAL   B N   1 
ATOM   4685 C CA  . VAL   B 1 259 ? -31.750 13.700  -3.239  1.00 33.29  ? 256 VAL   B CA  1 
ATOM   4686 C C   . VAL   B 1 259 ? -31.279 13.953  -4.666  1.00 40.61  ? 256 VAL   B C   1 
ATOM   4687 O O   . VAL   B 1 259 ? -30.078 14.141  -4.913  1.00 40.89  ? 256 VAL   B O   1 
ATOM   4688 C CB  . VAL   B 1 259 ? -31.697 14.996  -2.416  1.00 34.52  ? 256 VAL   B CB  1 
ATOM   4689 C CG1 . VAL   B 1 259 ? -32.369 16.114  -3.167  1.00 35.89  ? 256 VAL   B CG1 1 
ATOM   4690 C CG2 . VAL   B 1 259 ? -32.346 14.785  -1.079  1.00 31.40  ? 256 VAL   B CG2 1 
ATOM   4691 N N   . ALA   B 1 260 ? -32.220 13.962  -5.603  1.00 42.28  ? 257 ALA   B N   1 
ATOM   4692 C CA  . ALA   B 1 260 ? -31.955 14.335  -6.983  1.00 35.68  ? 257 ALA   B CA  1 
ATOM   4693 C C   . ALA   B 1 260 ? -32.712 15.620  -7.294  1.00 39.05  ? 257 ALA   B C   1 
ATOM   4694 O O   . ALA   B 1 260 ? -33.923 15.696  -7.080  1.00 39.60  ? 257 ALA   B O   1 
ATOM   4695 C CB  . ALA   B 1 260 ? -32.364 13.213  -7.940  1.00 36.11  ? 257 ALA   B CB  1 
ATOM   4696 N N   . VAL   B 1 261 ? -32.000 16.632  -7.775  1.00 37.69  ? 258 VAL   B N   1 
ATOM   4697 C CA  . VAL   B 1 261 ? -32.595 17.930  -8.074  1.00 39.41  ? 258 VAL   B CA  1 
ATOM   4698 C C   . VAL   B 1 261 ? -32.831 18.009  -9.577  1.00 37.05  ? 258 VAL   B C   1 
ATOM   4699 O O   . VAL   B 1 261 ? -31.889 18.087  -10.371 1.00 34.36  ? 258 VAL   B O   1 
ATOM   4700 C CB  . VAL   B 1 261 ? -31.728 19.099  -7.582  1.00 42.23  ? 258 VAL   B CB  1 
ATOM   4701 C CG1 . VAL   B 1 261 ? -32.398 20.407  -7.963  1.00 40.23  ? 258 VAL   B CG1 1 
ATOM   4702 C CG2 . VAL   B 1 261 ? -31.511 19.035  -6.058  1.00 34.25  ? 258 VAL   B CG2 1 
ATOM   4703 N N   . CYS   B 1 262 ? -34.101 18.002  -9.958  1.00 41.89  ? 259 CYS   B N   1 
ATOM   4704 C CA  . CYS   B 1 262 ? -34.549 18.041  -11.341 1.00 38.62  ? 259 CYS   B CA  1 
ATOM   4705 C C   . CYS   B 1 262 ? -34.940 19.443  -11.785 1.00 39.20  ? 259 CYS   B C   1 
ATOM   4706 O O   . CYS   B 1 262 ? -34.640 19.842  -12.916 1.00 39.85  ? 259 CYS   B O   1 
ATOM   4707 C CB  . CYS   B 1 262 ? -35.740 17.088  -11.516 1.00 38.84  ? 259 CYS   B CB  1 
ATOM   4708 S SG  . CYS   B 1 262 ? -36.162 16.733  -13.216 1.00 47.23  ? 259 CYS   B SG  1 
ATOM   4709 N N   . TRP   B 1 263 ? -35.587 20.203  -10.908 1.00 36.01  ? 260 TRP   B N   1 
ATOM   4710 C CA  . TRP   B 1 263 ? -35.987 21.567  -11.209 1.00 34.36  ? 260 TRP   B CA  1 
ATOM   4711 C C   . TRP   B 1 263 ? -36.220 22.295  -9.892  1.00 36.65  ? 260 TRP   B C   1 
ATOM   4712 O O   . TRP   B 1 263 ? -36.177 21.699  -8.815  1.00 36.90  ? 260 TRP   B O   1 
ATOM   4713 C CB  . TRP   B 1 263 ? -37.218 21.586  -12.134 1.00 40.63  ? 260 TRP   B CB  1 
ATOM   4714 C CG  . TRP   B 1 263 ? -37.103 22.663  -13.165 1.00 43.02  ? 260 TRP   B CG  1 
ATOM   4715 C CD1 . TRP   B 1 263 ? -36.061 22.862  -14.029 1.00 38.06  ? 260 TRP   B CD1 1 
ATOM   4716 C CD2 . TRP   B 1 263 ? -38.035 23.717  -13.414 1.00 39.69  ? 260 TRP   B CD2 1 
ATOM   4717 N NE1 . TRP   B 1 263 ? -36.291 23.974  -14.795 1.00 34.61  ? 260 TRP   B NE1 1 
ATOM   4718 C CE2 . TRP   B 1 263 ? -37.493 24.520  -14.436 1.00 36.81  ? 260 TRP   B CE2 1 
ATOM   4719 C CE3 . TRP   B 1 263 ? -39.279 24.054  -12.883 1.00 40.52  ? 260 TRP   B CE3 1 
ATOM   4720 C CZ2 . TRP   B 1 263 ? -38.156 25.630  -14.938 1.00 39.23  ? 260 TRP   B CZ2 1 
ATOM   4721 C CZ3 . TRP   B 1 263 ? -39.933 25.165  -13.378 1.00 41.75  ? 260 TRP   B CZ3 1 
ATOM   4722 C CH2 . TRP   B 1 263 ? -39.374 25.936  -14.396 1.00 40.56  ? 260 TRP   B CH2 1 
ATOM   4723 N N   . GLN   B 1 264 ? -36.424 23.605  -9.981  1.00 38.52  ? 261 GLN   B N   1 
ATOM   4724 C CA  . GLN   B 1 264 ? -36.718 24.421  -8.807  1.00 35.61  ? 261 GLN   B CA  1 
ATOM   4725 C C   . GLN   B 1 264 ? -37.820 25.421  -9.167  1.00 35.35  ? 261 GLN   B C   1 
ATOM   4726 O O   . GLN   B 1 264 ? -37.623 26.633  -9.156  1.00 31.90  ? 261 GLN   B O   1 
ATOM   4727 C CB  . GLN   B 1 264 ? -35.473 25.144  -8.295  1.00 35.74  ? 261 GLN   B CB  1 
ATOM   4728 C CG  . GLN   B 1 264 ? -34.355 24.236  -7.804  1.00 42.89  ? 261 GLN   B CG  1 
ATOM   4729 C CD  . GLN   B 1 264 ? -34.669 23.581  -6.464  1.00 38.99  ? 261 GLN   B CD  1 
ATOM   4730 O OE1 . GLN   B 1 264 ? -34.356 24.127  -5.404  1.00 43.24  ? 261 GLN   B OE1 1 
ATOM   4731 N NE2 . GLN   B 1 264 ? -35.292 22.413  -6.510  1.00 35.76  ? 261 GLN   B NE2 1 
ATOM   4732 N N   . TRP   B 1 265 ? -38.990 24.881  -9.518  1.00 33.96  ? 262 TRP   B N   1 
ATOM   4733 C CA  . TRP   B 1 265 ? -40.157 25.693  -9.850  1.00 36.04  ? 262 TRP   B CA  1 
ATOM   4734 C C   . TRP   B 1 265 ? -40.318 26.900  -8.932  1.00 39.32  ? 262 TRP   B C   1 
ATOM   4735 O O   . TRP   B 1 265 ? -40.524 28.029  -9.395  1.00 43.81  ? 262 TRP   B O   1 
ATOM   4736 C CB  . TRP   B 1 265 ? -41.404 24.816  -9.780  1.00 37.11  ? 262 TRP   B CB  1 
ATOM   4737 C CG  . TRP   B 1 265 ? -42.659 25.495  -10.238 1.00 39.25  ? 262 TRP   B CG  1 
ATOM   4738 C CD1 . TRP   B 1 265 ? -43.284 26.556  -9.652  1.00 34.37  ? 262 TRP   B CD1 1 
ATOM   4739 C CD2 . TRP   B 1 265 ? -43.461 25.132  -11.374 1.00 36.33  ? 262 TRP   B CD2 1 
ATOM   4740 N NE1 . TRP   B 1 265 ? -44.412 26.883  -10.361 1.00 37.19  ? 262 TRP   B NE1 1 
ATOM   4741 C CE2 . TRP   B 1 265 ? -44.547 26.017  -11.415 1.00 34.13  ? 262 TRP   B CE2 1 
ATOM   4742 C CE3 . TRP   B 1 265 ? -43.361 24.142  -12.353 1.00 33.91  ? 262 TRP   B CE3 1 
ATOM   4743 C CZ2 . TRP   B 1 265 ? -45.526 25.948  -12.403 1.00 38.44  ? 262 TRP   B CZ2 1 
ATOM   4744 C CZ3 . TRP   B 1 265 ? -44.335 24.070  -13.321 1.00 38.50  ? 262 TRP   B CZ3 1 
ATOM   4745 C CH2 . TRP   B 1 265 ? -45.400 24.971  -13.347 1.00 37.57  ? 262 TRP   B CH2 1 
ATOM   4746 N N   . ALA   B 1 266 ? -40.227 26.673  -7.618  1.00 40.67  ? 263 ALA   B N   1 
ATOM   4747 C CA  . ALA   B 1 266 ? -40.405 27.755  -6.656  1.00 41.78  ? 263 ALA   B CA  1 
ATOM   4748 C C   . ALA   B 1 266 ? -39.422 28.901  -6.884  1.00 41.00  ? 263 ALA   B C   1 
ATOM   4749 O O   . ALA   B 1 266 ? -39.741 30.059  -6.600  1.00 45.58  ? 263 ALA   B O   1 
ATOM   4750 C CB  . ALA   B 1 266 ? -40.267 27.208  -5.240  1.00 35.80  ? 263 ALA   B CB  1 
ATOM   4751 N N   . THR   B 1 267 ? -38.228 28.610  -7.378  1.00 37.29  ? 264 THR   B N   1 
ATOM   4752 C CA  . THR   B 1 267 ? -37.287 29.688  -7.632  1.00 40.56  ? 264 THR   B CA  1 
ATOM   4753 C C   . THR   B 1 267 ? -37.375 30.206  -9.060  1.00 40.54  ? 264 THR   B C   1 
ATOM   4754 O O   . THR   B 1 267 ? -37.369 31.419  -9.274  1.00 42.27  ? 264 THR   B O   1 
ATOM   4755 C CB  . THR   B 1 267 ? -35.869 29.218  -7.333  1.00 40.35  ? 264 THR   B CB  1 
ATOM   4756 O OG1 . THR   B 1 267 ? -35.786 28.843  -5.954  1.00 42.86  ? 264 THR   B OG1 1 
ATOM   4757 C CG2 . THR   B 1 267 ? -34.862 30.330  -7.622  1.00 38.69  ? 264 THR   B CG2 1 
ATOM   4758 N N   . GLN   B 1 268 ? -37.462 29.307  -10.042 1.00 40.34  ? 265 GLN   B N   1 
ATOM   4759 C CA  . GLN   B 1 268 ? -37.497 29.726  -11.440 1.00 40.50  ? 265 GLN   B CA  1 
ATOM   4760 C C   . GLN   B 1 268 ? -38.799 30.459  -11.767 1.00 44.67  ? 265 GLN   B C   1 
ATOM   4761 O O   . GLN   B 1 268 ? -38.774 31.561  -12.326 1.00 46.53  ? 265 GLN   B O   1 
ATOM   4762 C CB  . GLN   B 1 268 ? -37.301 28.516  -12.359 1.00 35.87  ? 265 GLN   B CB  1 
ATOM   4763 C CG  . GLN   B 1 268 ? -37.329 28.852  -13.842 1.00 39.65  ? 265 GLN   B CG  1 
ATOM   4764 C CD  . GLN   B 1 268 ? -36.231 29.840  -14.253 1.00 47.42  ? 265 GLN   B CD  1 
ATOM   4765 O OE1 . GLN   B 1 268 ? -35.094 29.758  -13.779 1.00 44.74  ? 265 GLN   B OE1 1 
ATOM   4766 N NE2 . GLN   B 1 268 ? -36.574 30.785  -15.133 1.00 47.02  ? 265 GLN   B NE2 1 
ATOM   4767 N N   . VAL   B 1 269 ? -39.939 29.923  -11.380 1.00 43.17  ? 266 VAL   B N   1 
ATOM   4768 C CA  . VAL   B 1 269 ? -41.201 30.550  -11.741 1.00 40.75  ? 266 VAL   B CA  1 
ATOM   4769 C C   . VAL   B 1 269 ? -41.744 31.468  -10.651 1.00 44.13  ? 266 VAL   B C   1 
ATOM   4770 O O   . VAL   B 1 269 ? -42.165 32.576  -10.936 1.00 39.03  ? 266 VAL   B O   1 
ATOM   4771 C CB  . VAL   B 1 269 ? -42.254 29.482  -12.110 1.00 42.54  ? 266 VAL   B CB  1 
ATOM   4772 C CG1 . VAL   B 1 269 ? -43.597 30.118  -12.414 1.00 37.55  ? 266 VAL   B CG1 1 
ATOM   4773 C CG2 . VAL   B 1 269 ? -41.775 28.633  -13.269 1.00 40.05  ? 266 VAL   B CG2 1 
ATOM   4774 N N   . GLN   B 1 270 ? -41.722 31.019  -9.403  1.00 43.95  ? 267 GLN   B N   1 
ATOM   4775 C CA  . GLN   B 1 270 ? -42.307 31.804  -8.309  1.00 43.68  ? 267 GLN   B CA  1 
ATOM   4776 C C   . GLN   B 1 270 ? -41.329 32.783  -7.677  1.00 42.23  ? 267 GLN   B C   1 
ATOM   4777 O O   . GLN   B 1 270 ? -41.671 33.459  -6.725  1.00 45.53  ? 267 GLN   B O   1 
ATOM   4778 C CB  . GLN   B 1 270 ? -42.910 30.877  -7.273  1.00 40.90  ? 267 GLN   B CB  1 
ATOM   4779 C CG  . GLN   B 1 270 ? -43.670 29.701  -7.840  1.00 48.36  ? 267 GLN   B CG  1 
ATOM   4780 C CD  . GLN   B 1 270 ? -44.331 28.886  -6.750  1.00 54.23  ? 267 GLN   B CD  1 
ATOM   4781 O OE1 . GLN   B 1 270 ? -43.817 27.852  -6.334  1.00 56.72  ? 267 GLN   B OE1 1 
ATOM   4782 N NE2 . GLN   B 1 270 ? -45.474 29.357  -6.273  1.00 49.02  ? 267 GLN   B NE2 1 
ATOM   4783 N N   . ARG   B 1 271 ? -40.124 32.858  -8.201  1.00 45.56  ? 268 ARG   B N   1 
ATOM   4784 C CA  . ARG   B 1 271 ? -39.112 33.816  -7.740  1.00 47.55  ? 268 ARG   B CA  1 
ATOM   4785 C C   . ARG   B 1 271 ? -38.769 33.816  -6.256  1.00 50.37  ? 268 ARG   B C   1 
ATOM   4786 O O   . ARG   B 1 271 ? -38.443 34.850  -5.700  1.00 52.40  ? 268 ARG   B O   1 
ATOM   4787 C CB  . ARG   B 1 271 ? -39.502 35.197  -8.233  1.00 45.49  ? 268 ARG   B CB  1 
ATOM   4788 C CG  . ARG   B 1 271 ? -39.980 35.168  -9.676  1.00 53.87  ? 268 ARG   B CG  1 
ATOM   4789 C CD  . ARG   B 1 271 ? -40.152 36.557  -10.251 1.00 51.33  ? 268 ARG   B CD  1 
ATOM   4790 N NE  . ARG   B 1 271 ? -38.872 37.167  -10.580 1.00 59.38  ? 268 ARG   B NE  1 
ATOM   4791 C CZ  . ARG   B 1 271 ? -38.727 38.429  -10.960 1.00 57.67  ? 268 ARG   B CZ  1 
ATOM   4792 N NH1 . ARG   B 1 271 ? -39.786 39.215  -11.060 1.00 49.56  ? 268 ARG   B NH1 1 
ATOM   4793 N NH2 . ARG   B 1 271 ? -37.525 38.902  -11.242 1.00 59.05  ? 268 ARG   B NH2 1 
ATOM   4794 N N   . ASP   B 1 272 ? -38.804 32.656  -5.629  1.00 46.67  ? 269 ASP   B N   1 
ATOM   4795 C CA  . ASP   B 1 272 ? -38.396 32.532  -4.225  1.00 50.77  ? 269 ASP   B CA  1 
ATOM   4796 C C   . ASP   B 1 272 ? -36.903 32.226  -4.190  1.00 50.20  ? 269 ASP   B C   1 
ATOM   4797 O O   . ASP   B 1 272 ? -36.484 31.080  -4.363  1.00 48.52  ? 269 ASP   B O   1 
ATOM   4798 C CB  . ASP   B 1 272 ? -39.207 31.449  -3.521  1.00 50.96  ? 269 ASP   B CB  1 
ATOM   4799 C CG  . ASP   B 1 272 ? -39.061 31.483  -1.993  1.00 61.81  ? 269 ASP   B CG  1 
ATOM   4800 O OD1 . ASP   B 1 272 ? -38.691 32.550  -1.430  1.00 61.37  ? 269 ASP   B OD1 1 
ATOM   4801 O OD2 . ASP   B 1 272 ? -39.313 30.432  -1.356  1.00 61.19  ? 269 ASP   B OD2 1 
ATOM   4802 N N   . TYR   B 1 273 ? -36.092 33.251  -3.965  1.00 50.39  ? 270 TYR   B N   1 
ATOM   4803 C CA  . TYR   B 1 273 ? -34.653 33.084  -4.072  1.00 53.52  ? 270 TYR   B CA  1 
ATOM   4804 C C   . TYR   B 1 273 ? -33.974 32.825  -2.739  1.00 49.44  ? 270 TYR   B C   1 
ATOM   4805 O O   . TYR   B 1 273 ? -32.844 32.329  -2.724  1.00 48.02  ? 270 TYR   B O   1 
ATOM   4806 C CB  . TYR   B 1 273 ? -34.028 34.321  -4.722  1.00 53.10  ? 270 TYR   B CB  1 
ATOM   4807 C CG  . TYR   B 1 273 ? -34.587 34.616  -6.086  1.00 56.24  ? 270 TYR   B CG  1 
ATOM   4808 C CD1 . TYR   B 1 273 ? -34.492 33.686  -7.111  1.00 55.26  ? 270 TYR   B CD1 1 
ATOM   4809 C CD2 . TYR   B 1 273 ? -35.208 35.831  -6.358  1.00 62.97  ? 270 TYR   B CD2 1 
ATOM   4810 C CE1 . TYR   B 1 273 ? -35.011 33.950  -8.369  1.00 55.46  ? 270 TYR   B CE1 1 
ATOM   4811 C CE2 . TYR   B 1 273 ? -35.728 36.107  -7.620  1.00 56.97  ? 270 TYR   B CE2 1 
ATOM   4812 C CZ  . TYR   B 1 273 ? -35.629 35.159  -8.616  1.00 57.97  ? 270 TYR   B CZ  1 
ATOM   4813 O OH  . TYR   B 1 273 ? -36.144 35.414  -9.870  1.00 61.91  ? 270 TYR   B OH  1 
ATOM   4814 N N   . HIS   B 1 274 ? -34.620 33.154  -1.628  1.00 55.23  ? 271 HIS   B N   1 
ATOM   4815 C CA  . HIS   B 1 274 ? -34.024 32.977  -0.314  1.00 52.11  ? 271 HIS   B CA  1 
ATOM   4816 C C   . HIS   B 1 274 ? -34.896 32.065  0.536   1.00 51.11  ? 271 HIS   B C   1 
ATOM   4817 O O   . HIS   B 1 274 ? -36.103 31.905  0.299   1.00 54.16  ? 271 HIS   B O   1 
ATOM   4818 C CB  . HIS   B 1 274 ? -33.788 34.324  0.379   1.00 46.54  ? 271 HIS   B CB  1 
ATOM   4819 C CG  . HIS   B 1 274 ? -32.803 35.194  -0.341  1.00 63.45  ? 271 HIS   B CG  1 
ATOM   4820 N ND1 . HIS   B 1 274 ? -32.957 35.557  -1.666  1.00 65.88  ? 271 HIS   B ND1 1 
ATOM   4821 C CD2 . HIS   B 1 274 ? -31.639 35.757  0.069   1.00 67.05  ? 271 HIS   B CD2 1 
ATOM   4822 C CE1 . HIS   B 1 274 ? -31.939 36.317  -2.035  1.00 64.95  ? 271 HIS   B CE1 1 
ATOM   4823 N NE2 . HIS   B 1 274 ? -31.123 36.452  -1.003  1.00 67.03  ? 271 HIS   B NE2 1 
ATOM   4824 N N   . GLY   B 1 275 ? -34.240 31.445  1.514   1.00 48.42  ? 272 GLY   B N   1 
ATOM   4825 C CA  . GLY   B 1 275 ? -34.831 30.431  2.349   1.00 43.19  ? 272 GLY   B CA  1 
ATOM   4826 C C   . GLY   B 1 275 ? -33.853 29.930  3.395   1.00 46.46  ? 272 GLY   B C   1 
ATOM   4827 O O   . GLY   B 1 275 ? -32.712 30.399  3.506   1.00 42.01  ? 272 GLY   B O   1 
ATOM   4828 N N   . PRO   B 1 276 ? -34.298 28.975  4.205   1.00 54.09  ? 273 PRO   B N   1 
ATOM   4829 C CA  . PRO   B 1 276 ? -33.394 28.367  5.187   1.00 50.85  ? 273 PRO   B CA  1 
ATOM   4830 C C   . PRO   B 1 276 ? -32.212 27.696  4.502   1.00 46.27  ? 273 PRO   B C   1 
ATOM   4831 O O   . PRO   B 1 276 ? -32.351 27.057  3.460   1.00 47.48  ? 273 PRO   B O   1 
ATOM   4832 C CB  . PRO   B 1 276 ? -34.287 27.343  5.897   1.00 45.71  ? 273 PRO   B CB  1 
ATOM   4833 C CG  . PRO   B 1 276 ? -35.393 27.060  4.901   1.00 45.36  ? 273 PRO   B CG  1 
ATOM   4834 C CD  . PRO   B 1 276 ? -35.647 28.381  4.259   1.00 48.50  ? 273 PRO   B CD  1 
ATOM   4835 N N   . ARG   B 1 277 ? -31.038 27.844  5.096   1.00 48.37  ? 274 ARG   B N   1 
ATOM   4836 C CA  . ARG   B 1 277 ? -29.873 27.151  4.579   1.00 43.79  ? 274 ARG   B CA  1 
ATOM   4837 C C   . ARG   B 1 277 ? -30.021 25.651  4.796   1.00 45.21  ? 274 ARG   B C   1 
ATOM   4838 O O   . ARG   B 1 277 ? -30.282 25.201  5.912   1.00 43.15  ? 274 ARG   B O   1 
ATOM   4839 C CB  . ARG   B 1 277 ? -28.627 27.674  5.257   1.00 44.11  ? 274 ARG   B CB  1 
ATOM   4840 C CG  . ARG   B 1 277 ? -28.403 29.142  4.997   1.00 45.80  ? 274 ARG   B CG  1 
ATOM   4841 C CD  . ARG   B 1 277 ? -27.011 29.488  5.428   1.00 51.05  ? 274 ARG   B CD  1 
ATOM   4842 N NE  . ARG   B 1 277 ? -26.671 30.884  5.191   1.00 55.57  ? 274 ARG   B NE  1 
ATOM   4843 C CZ  . ARG   B 1 277 ? -26.267 31.365  4.024   1.00 50.84  ? 274 ARG   B CZ  1 
ATOM   4844 N NH1 . ARG   B 1 277 ? -26.294 30.624  2.922   1.00 54.27  ? 274 ARG   B NH1 1 
ATOM   4845 N NH2 . ARG   B 1 277 ? -25.822 32.614  3.963   1.00 45.03  ? 274 ARG   B NH2 1 
ATOM   4846 N N   . LEU   B 1 278 ? -29.868 24.880  3.716   1.00 48.31  ? 275 LEU   B N   1 
ATOM   4847 C CA  . LEU   B 1 278 ? -30.159 23.451  3.729   1.00 44.13  ? 275 LEU   B CA  1 
ATOM   4848 C C   . LEU   B 1 278 ? -28.942 22.579  4.015   1.00 43.12  ? 275 LEU   B C   1 
ATOM   4849 O O   . LEU   B 1 278 ? -29.094 21.517  4.633   1.00 41.13  ? 275 LEU   B O   1 
ATOM   4850 C CB  . LEU   B 1 278 ? -30.773 23.026  2.391   1.00 38.85  ? 275 LEU   B CB  1 
ATOM   4851 C CG  . LEU   B 1 278 ? -32.136 23.648  2.091   1.00 41.89  ? 275 LEU   B CG  1 
ATOM   4852 C CD1 . LEU   B 1 278 ? -32.633 23.227  0.728   1.00 38.96  ? 275 LEU   B CD1 1 
ATOM   4853 C CD2 . LEU   B 1 278 ? -33.129 23.241  3.153   1.00 43.51  ? 275 LEU   B CD2 1 
ATOM   4854 N N   . LEU   B 1 279 ? -27.751 22.978  3.567   1.00 39.69  ? 276 LEU   B N   1 
ATOM   4855 C CA  . LEU   B 1 279 ? -26.554 22.178  3.819   1.00 38.64  ? 276 LEU   B CA  1 
ATOM   4856 C C   . LEU   B 1 279 ? -26.347 21.796  5.290   1.00 40.39  ? 276 LEU   B C   1 
ATOM   4857 O O   . LEU   B 1 279 ? -25.877 20.675  5.539   1.00 34.71  ? 276 LEU   B O   1 
ATOM   4858 C CB  . LEU   B 1 279 ? -25.311 22.911  3.288   1.00 42.68  ? 276 LEU   B CB  1 
ATOM   4859 C CG  . LEU   B 1 279 ? -25.224 23.354  1.822   1.00 40.49  ? 276 LEU   B CG  1 
ATOM   4860 C CD1 . LEU   B 1 279 ? -23.823 23.865  1.531   1.00 36.32  ? 276 LEU   B CD1 1 
ATOM   4861 C CD2 . LEU   B 1 279 ? -25.602 22.250  0.868   1.00 34.79  ? 276 LEU   B CD2 1 
ATOM   4862 N N   . PRO   B 1 280 ? -26.665 22.629  6.291   1.00 41.79  ? 277 PRO   B N   1 
ATOM   4863 C CA  . PRO   B 1 280 ? -26.547 22.155  7.684   1.00 36.56  ? 277 PRO   B CA  1 
ATOM   4864 C C   . PRO   B 1 280 ? -27.312 20.870  7.997   1.00 38.47  ? 277 PRO   B C   1 
ATOM   4865 O O   . PRO   B 1 280 ? -26.989 20.209  8.987   1.00 48.44  ? 277 PRO   B O   1 
ATOM   4866 C CB  . PRO   B 1 280 ? -27.092 23.333  8.500   1.00 34.99  ? 277 PRO   B CB  1 
ATOM   4867 C CG  . PRO   B 1 280 ? -26.715 24.531  7.681   1.00 40.01  ? 277 PRO   B CG  1 
ATOM   4868 C CD  . PRO   B 1 280 ? -26.918 24.087  6.244   1.00 39.57  ? 277 PRO   B CD  1 
ATOM   4869 N N   . TYR   B 1 281 ? -28.293 20.476  7.206   1.00 39.54  ? 278 TYR   B N   1 
ATOM   4870 C CA  . TYR   B 1 281 ? -29.138 19.344  7.566   1.00 38.14  ? 278 TYR   B CA  1 
ATOM   4871 C C   . TYR   B 1 281 ? -28.659 18.031  6.991   1.00 37.68  ? 278 TYR   B C   1 
ATOM   4872 O O   . TYR   B 1 281 ? -29.275 16.996  7.254   1.00 42.55  ? 278 TYR   B O   1 
ATOM   4873 C CB  . TYR   B 1 281 ? -30.572 19.580  7.092   1.00 40.77  ? 278 TYR   B CB  1 
ATOM   4874 C CG  . TYR   B 1 281 ? -31.271 20.642  7.881   1.00 45.96  ? 278 TYR   B CG  1 
ATOM   4875 C CD1 . TYR   B 1 281 ? -31.150 21.983  7.533   1.00 40.98  ? 278 TYR   B CD1 1 
ATOM   4876 C CD2 . TYR   B 1 281 ? -32.045 20.307  8.993   1.00 47.88  ? 278 TYR   B CD2 1 
ATOM   4877 C CE1 . TYR   B 1 281 ? -31.794 22.965  8.264   1.00 52.45  ? 278 TYR   B CE1 1 
ATOM   4878 C CE2 . TYR   B 1 281 ? -32.687 21.275  9.731   1.00 48.45  ? 278 TYR   B CE2 1 
ATOM   4879 C CZ  . TYR   B 1 281 ? -32.564 22.601  9.367   1.00 54.98  ? 278 TYR   B CZ  1 
ATOM   4880 O OH  . TYR   B 1 281 ? -33.210 23.563  10.114  1.00 59.26  ? 278 TYR   B OH  1 
ATOM   4881 N N   . ILE   B 1 282 ? -27.602 18.039  6.194   1.00 37.09  ? 279 ILE   B N   1 
ATOM   4882 C CA  . ILE   B 1 282 ? -27.236 16.855  5.431   1.00 36.63  ? 279 ILE   B CA  1 
ATOM   4883 C C   . ILE   B 1 282 ? -26.013 16.164  5.973   1.00 32.25  ? 279 ILE   B C   1 
ATOM   4884 O O   . ILE   B 1 282 ? -25.716 15.049  5.524   1.00 36.22  ? 279 ILE   B O   1 
ATOM   4885 C CB  . ILE   B 1 282 ? -27.035 17.182  3.935   1.00 32.72  ? 279 ILE   B CB  1 
ATOM   4886 C CG1 . ILE   B 1 282 ? -25.690 17.881  3.706   1.00 29.68  ? 279 ILE   B CG1 1 
ATOM   4887 C CG2 . ILE   B 1 282 ? -28.223 17.999  3.423   1.00 33.55  ? 279 ILE   B CG2 1 
ATOM   4888 C CD1 . ILE   B 1 282 ? -25.207 17.848  2.260   1.00 32.11  ? 279 ILE   B CD1 1 
ATOM   4889 N N   . MET   B 1 283 ? -25.306 16.766  6.930   1.00 36.48  ? 280 MET   B N   1 
ATOM   4890 C CA  . MET   B 1 283 ? -24.048 16.191  7.408   1.00 36.96  ? 280 MET   B CA  1 
ATOM   4891 C C   . MET   B 1 283 ? -24.284 14.915  8.192   1.00 35.42  ? 280 MET   B C   1 
ATOM   4892 O O   . MET   B 1 283 ? -23.657 13.883  7.917   1.00 37.48  ? 280 MET   B O   1 
ATOM   4893 C CB  . MET   B 1 283 ? -23.297 17.200  8.271   1.00 38.92  ? 280 MET   B CB  1 
ATOM   4894 C CG  . MET   B 1 283 ? -22.965 18.472  7.534   1.00 36.57  ? 280 MET   B CG  1 
ATOM   4895 S SD  . MET   B 1 283 ? -22.150 19.664  8.568   1.00 45.43  ? 280 MET   B SD  1 
ATOM   4896 C CE  . MET   B 1 283 ? -23.572 20.448  9.319   1.00 42.02  ? 280 MET   B CE  1 
ATOM   4897 N N   . PHE   B 1 284 ? -25.176 14.959  9.175   1.00 37.61  ? 281 PHE   B N   1 
ATOM   4898 C CA  . PHE   B 1 284 ? -25.383 13.750  9.967   1.00 39.55  ? 281 PHE   B CA  1 
ATOM   4899 C C   . PHE   B 1 284 ? -26.042 12.659  9.134   1.00 40.50  ? 281 PHE   B C   1 
ATOM   4900 O O   . PHE   B 1 284 ? -25.648 11.487  9.261   1.00 40.15  ? 281 PHE   B O   1 
ATOM   4901 C CB  . PHE   B 1 284 ? -26.214 13.999  11.236  1.00 41.64  ? 281 PHE   B CB  1 
ATOM   4902 C CG  . PHE   B 1 284 ? -26.600 12.724  11.932  1.00 46.34  ? 281 PHE   B CG  1 
ATOM   4903 C CD1 . PHE   B 1 284 ? -25.720 12.117  12.833  1.00 45.97  ? 281 PHE   B CD1 1 
ATOM   4904 C CD2 . PHE   B 1 284 ? -27.809 12.087  11.643  1.00 43.50  ? 281 PHE   B CD2 1 
ATOM   4905 C CE1 . PHE   B 1 284 ? -26.045 10.914  13.447  1.00 42.85  ? 281 PHE   B CE1 1 
ATOM   4906 C CE2 . PHE   B 1 284 ? -28.135 10.880  12.257  1.00 46.00  ? 281 PHE   B CE2 1 
ATOM   4907 C CZ  . PHE   B 1 284 ? -27.252 10.296  13.159  1.00 44.42  ? 281 PHE   B CZ  1 
ATOM   4908 N N   . PRO   B 1 285 ? -27.053 12.964  8.307   1.00 40.30  ? 282 PRO   B N   1 
ATOM   4909 C CA  . PRO   B 1 285 ? -27.630 11.910  7.454   1.00 37.71  ? 282 PRO   B CA  1 
ATOM   4910 C C   . PRO   B 1 285 ? -26.673 11.365  6.429   1.00 39.53  ? 282 PRO   B C   1 
ATOM   4911 O O   . PRO   B 1 285 ? -26.980 10.327  5.822   1.00 37.03  ? 282 PRO   B O   1 
ATOM   4912 C CB  . PRO   B 1 285 ? -28.799 12.616  6.761   1.00 38.77  ? 282 PRO   B CB  1 
ATOM   4913 C CG  . PRO   B 1 285 ? -29.140 13.750  7.661   1.00 36.91  ? 282 PRO   B CG  1 
ATOM   4914 C CD  . PRO   B 1 285 ? -27.841 14.209  8.224   1.00 39.70  ? 282 PRO   B CD  1 
ATOM   4915 N N   . ARG   B 1 286 ? -25.525 12.017  6.226   1.00 35.56  ? 283 ARG   B N   1 
ATOM   4916 C CA  . ARG   B 1 286 ? -24.675 11.749  5.065   1.00 35.67  ? 283 ARG   B CA  1 
ATOM   4917 C C   . ARG   B 1 286 ? -25.510 11.720  3.785   1.00 32.60  ? 283 ARG   B C   1 
ATOM   4918 O O   . ARG   B 1 286 ? -25.480 10.768  3.007   1.00 31.41  ? 283 ARG   B O   1 
ATOM   4919 C CB  . ARG   B 1 286 ? -23.894 10.448  5.242   1.00 35.93  ? 283 ARG   B CB  1 
ATOM   4920 C CG  . ARG   B 1 286 ? -22.949 10.480  6.425   1.00 38.70  ? 283 ARG   B CG  1 
ATOM   4921 C CD  . ARG   B 1 286 ? -23.081 9.225   7.254   1.00 34.14  ? 283 ARG   B CD  1 
ATOM   4922 N NE  . ARG   B 1 286 ? -23.953 9.447   8.392   1.00 36.99  ? 283 ARG   B NE  1 
ATOM   4923 C CZ  . ARG   B 1 286 ? -24.336 8.497   9.232   1.00 38.11  ? 283 ARG   B CZ  1 
ATOM   4924 N NH1 . ARG   B 1 286 ? -24.007 7.228   9.031   1.00 30.05  ? 283 ARG   B NH1 1 
ATOM   4925 N NH2 . ARG   B 1 286 ? -25.068 8.829   10.297  1.00 34.49  ? 283 ARG   B NH2 1 
ATOM   4926 N N   . ALA   B 1 287 ? -26.285 12.777  3.580   1.00 32.48  ? 284 ALA   B N   1 
ATOM   4927 C CA  . ALA   B 1 287 ? -27.126 12.838  2.398   1.00 35.65  ? 284 ALA   B CA  1 
ATOM   4928 C C   . ALA   B 1 287 ? -26.280 13.088  1.154   1.00 34.64  ? 284 ALA   B C   1 
ATOM   4929 O O   . ALA   B 1 287 ? -25.263 13.790  1.195   1.00 31.08  ? 284 ALA   B O   1 
ATOM   4930 C CB  . ALA   B 1 287 ? -28.174 13.932  2.569   1.00 33.56  ? 284 ALA   B CB  1 
ATOM   4931 N N   . THR   B 1 288 ? -26.686 12.499  0.043   1.00 31.33  ? 285 THR   B N   1 
ATOM   4932 C CA  . THR   B 1 288 ? -26.080 12.817  -1.243  1.00 35.80  ? 285 THR   B CA  1 
ATOM   4933 C C   . THR   B 1 288 ? -27.101 13.556  -2.098  1.00 37.15  ? 285 THR   B C   1 
ATOM   4934 O O   . THR   B 1 288 ? -28.232 13.089  -2.257  1.00 39.04  ? 285 THR   B O   1 
ATOM   4935 C CB  . THR   B 1 288 ? -25.569 11.563  -1.944  1.00 35.55  ? 285 THR   B CB  1 
ATOM   4936 O OG1 . THR   B 1 288 ? -24.555 10.961  -1.128  1.00 42.27  ? 285 THR   B OG1 1 
ATOM   4937 C CG2 . THR   B 1 288 ? -24.976 11.917  -3.294  1.00 33.69  ? 285 THR   B CG2 1 
ATOM   4938 N N   . ILE   B 1 289 ? -26.708 14.722  -2.611  1.00 33.70  ? 286 ILE   B N   1 
ATOM   4939 C CA  . ILE   B 1 289 ? -27.572 15.594  -3.404  1.00 33.48  ? 286 ILE   B CA  1 
ATOM   4940 C C   . ILE   B 1 289 ? -26.908 15.759  -4.757  1.00 34.41  ? 286 ILE   B C   1 
ATOM   4941 O O   . ILE   B 1 289 ? -25.780 16.264  -4.833  1.00 34.06  ? 286 ILE   B O   1 
ATOM   4942 C CB  . ILE   B 1 289 ? -27.771 16.960  -2.728  1.00 31.37  ? 286 ILE   B CB  1 
ATOM   4943 C CG1 . ILE   B 1 289 ? -28.138 16.764  -1.272  1.00 32.96  ? 286 ILE   B CG1 1 
ATOM   4944 C CG2 . ILE   B 1 289 ? -28.865 17.743  -3.390  1.00 32.10  ? 286 ILE   B CG2 1 
ATOM   4945 C CD1 . ILE   B 1 289 ? -28.103 18.026  -0.503  1.00 36.91  ? 286 ILE   B CD1 1 
ATOM   4946 N N   . ARG   B 1 290 ? -27.577 15.313  -5.819  1.00 32.93  ? 287 ARG   B N   1 
ATOM   4947 C CA  . ARG   B 1 290 ? -27.023 15.403  -7.166  1.00 30.79  ? 287 ARG   B CA  1 
ATOM   4948 C C   . ARG   B 1 290 ? -27.938 16.214  -8.074  1.00 33.90  ? 287 ARG   B C   1 
ATOM   4949 O O   . ARG   B 1 290 ? -29.125 15.900  -8.209  1.00 34.08  ? 287 ARG   B O   1 
ATOM   4950 C CB  . ARG   B 1 290 ? -26.807 14.028  -7.782  1.00 27.34  ? 287 ARG   B CB  1 
ATOM   4951 C CG  . ARG   B 1 290 ? -26.003 14.117  -9.048  1.00 32.96  ? 287 ARG   B CG  1 
ATOM   4952 C CD  . ARG   B 1 290 ? -26.173 12.881  -9.881  1.00 37.51  ? 287 ARG   B CD  1 
ATOM   4953 N NE  . ARG   B 1 290 ? -25.190 12.793  -10.958 1.00 37.76  ? 287 ARG   B NE  1 
ATOM   4954 C CZ  . ARG   B 1 290 ? -25.304 13.406  -12.128 1.00 38.02  ? 287 ARG   B CZ  1 
ATOM   4955 N NH1 . ARG   B 1 290 ? -26.289 14.263  -12.366 1.00 38.22  ? 287 ARG   B NH1 1 
ATOM   4956 N NH2 . ARG   B 1 290 ? -24.415 13.149  -13.085 1.00 38.15  ? 287 ARG   B NH2 1 
ATOM   4957 N N   . GLY   B 1 291 ? -27.382 17.239  -8.711  1.00 33.83  ? 288 GLY   B N   1 
ATOM   4958 C CA  . GLY   B 1 291 ? -28.133 17.966  -9.722  1.00 31.40  ? 288 GLY   B CA  1 
ATOM   4959 C C   . GLY   B 1 291 ? -28.305 17.133  -10.983 1.00 31.95  ? 288 GLY   B C   1 
ATOM   4960 O O   . GLY   B 1 291 ? -27.392 16.431  -11.426 1.00 33.14  ? 288 GLY   B O   1 
ATOM   4961 N N   . ILE   B 1 292 ? -29.500 17.198  -11.556 1.00 34.16  ? 289 ILE   B N   1 
ATOM   4962 C CA  . ILE   B 1 292 ? -29.838 16.427  -12.750 1.00 32.88  ? 289 ILE   B CA  1 
ATOM   4963 C C   . ILE   B 1 292 ? -29.785 17.340  -13.960 1.00 33.23  ? 289 ILE   B C   1 
ATOM   4964 O O   . ILE   B 1 292 ? -30.272 18.479  -13.929 1.00 31.83  ? 289 ILE   B O   1 
ATOM   4965 C CB  . ILE   B 1 292 ? -31.227 15.771  -12.630 1.00 31.43  ? 289 ILE   B CB  1 
ATOM   4966 C CG1 . ILE   B 1 292 ? -31.296 14.897  -11.376 1.00 33.21  ? 289 ILE   B CG1 1 
ATOM   4967 C CG2 . ILE   B 1 292 ? -31.531 14.946  -13.857 1.00 33.40  ? 289 ILE   B CG2 1 
ATOM   4968 C CD1 . ILE   B 1 292 ? -30.359 13.717  -11.383 1.00 25.18  ? 289 ILE   B CD1 1 
ATOM   4969 N N   . PHE   B 1 293 ? -29.212 16.828  -15.039 1.00 35.27  ? 290 PHE   B N   1 
ATOM   4970 C CA  . PHE   B 1 293 ? -29.197 17.553  -16.285 1.00 29.43  ? 290 PHE   B CA  1 
ATOM   4971 C C   . PHE   B 1 293 ? -29.114 16.488  -17.381 1.00 30.89  ? 290 PHE   B C   1 
ATOM   4972 O O   . PHE   B 1 293 ? -28.056 16.177  -17.938 1.00 31.90  ? 290 PHE   B O   1 
ATOM   4973 C CB  . PHE   B 1 293 ? -28.053 18.557  -16.340 1.00 30.15  ? 290 PHE   B CB  1 
ATOM   4974 C CG  . PHE   B 1 293 ? -28.177 19.515  -17.468 1.00 31.87  ? 290 PHE   B CG  1 
ATOM   4975 C CD1 . PHE   B 1 293 ? -29.122 20.547  -17.425 1.00 36.13  ? 290 PHE   B CD1 1 
ATOM   4976 C CD2 . PHE   B 1 293 ? -27.385 19.369  -18.607 1.00 31.98  ? 290 PHE   B CD2 1 
ATOM   4977 C CE1 . PHE   B 1 293 ? -29.257 21.438  -18.509 1.00 37.35  ? 290 PHE   B CE1 1 
ATOM   4978 C CE2 . PHE   B 1 293 ? -27.521 20.242  -19.673 1.00 32.45  ? 290 PHE   B CE2 1 
ATOM   4979 C CZ  . PHE   B 1 293 ? -28.462 21.284  -19.623 1.00 32.86  ? 290 PHE   B CZ  1 
ATOM   4980 N N   . SER   B 1 294 ? -30.273 15.907  -17.683 1.00 34.02  ? 291 SER   B N   1 
ATOM   4981 C CA  . SER   B 1 294 ? -30.360 14.682  -18.468 1.00 35.18  ? 291 SER   B CA  1 
ATOM   4982 C C   . SER   B 1 294 ? -29.752 14.799  -19.864 1.00 33.95  ? 291 SER   B C   1 
ATOM   4983 O O   . SER   B 1 294 ? -29.551 13.768  -20.515 1.00 34.17  ? 291 SER   B O   1 
ATOM   4984 C CB  . SER   B 1 294 ? -31.821 14.247  -18.552 1.00 39.38  ? 291 SER   B CB  1 
ATOM   4985 O OG  . SER   B 1 294 ? -32.644 15.359  -18.869 1.00 42.98  ? 291 SER   B OG  1 
ATOM   4986 N N   . LEU   B 1 295 ? -29.419 16.002  -20.332 1.00 35.27  ? 292 LEU   B N   1 
ATOM   4987 C CA  . LEU   B 1 295 ? -28.707 16.106  -21.599 1.00 35.05  ? 292 LEU   B CA  1 
ATOM   4988 C C   . LEU   B 1 295 ? -27.436 15.264  -21.630 1.00 35.18  ? 292 LEU   B C   1 
ATOM   4989 O O   . LEU   B 1 295 ? -26.987 14.872  -22.714 1.00 38.80  ? 292 LEU   B O   1 
ATOM   4990 C CB  . LEU   B 1 295 ? -28.342 17.563  -21.905 1.00 33.31  ? 292 LEU   B CB  1 
ATOM   4991 C CG  . LEU   B 1 295 ? -29.347 18.475  -22.611 1.00 33.45  ? 292 LEU   B CG  1 
ATOM   4992 C CD1 . LEU   B 1 295 ? -28.597 19.586  -23.335 1.00 36.94  ? 292 LEU   B CD1 1 
ATOM   4993 C CD2 . LEU   B 1 295 ? -30.217 17.719  -23.580 1.00 40.06  ? 292 LEU   B CD2 1 
ATOM   4994 N N   . GLU   B 1 296 ? -26.841 14.973  -20.473 1.00 37.80  ? 293 GLU   B N   1 
ATOM   4995 C CA  . GLU   B 1 296 ? -25.621 14.179  -20.468 1.00 37.23  ? 293 GLU   B CA  1 
ATOM   4996 C C   . GLU   B 1 296 ? -25.877 12.719  -20.811 1.00 39.14  ? 293 GLU   B C   1 
ATOM   4997 O O   . GLU   B 1 296 ? -24.921 11.999  -21.123 1.00 42.13  ? 293 GLU   B O   1 
ATOM   4998 C CB  . GLU   B 1 296 ? -24.933 14.263  -19.111 1.00 35.05  ? 293 GLU   B CB  1 
ATOM   4999 C CG  . GLU   B 1 296 ? -25.715 13.577  -18.023 1.00 38.47  ? 293 GLU   B CG  1 
ATOM   5000 C CD  . GLU   B 1 296 ? -24.950 13.512  -16.726 1.00 35.99  ? 293 GLU   B CD  1 
ATOM   5001 O OE1 . GLU   B 1 296 ? -23.708 13.541  -16.794 1.00 41.51  ? 293 GLU   B OE1 1 
ATOM   5002 O OE2 . GLU   B 1 296 ? -25.583 13.454  -15.646 1.00 39.47  ? 293 GLU   B OE2 1 
ATOM   5003 N N   . TRP   B 1 297 ? -27.130 12.271  -20.763 1.00 38.03  ? 294 TRP   B N   1 
ATOM   5004 C CA  . TRP   B 1 297 ? -27.493 10.891  -21.071 1.00 40.55  ? 294 TRP   B CA  1 
ATOM   5005 C C   . TRP   B 1 297 ? -27.972 10.696  -22.512 1.00 42.28  ? 294 TRP   B C   1 
ATOM   5006 O O   . TRP   B 1 297 ? -28.212 9.556   -22.925 1.00 41.85  ? 294 TRP   B O   1 
ATOM   5007 C CB  . TRP   B 1 297 ? -28.558 10.416  -20.076 1.00 38.54  ? 294 TRP   B CB  1 
ATOM   5008 C CG  . TRP   B 1 297 ? -28.060 10.466  -18.664 1.00 37.13  ? 294 TRP   B CG  1 
ATOM   5009 C CD1 . TRP   B 1 297 ? -26.771 10.242  -18.237 1.00 36.62  ? 294 TRP   B CD1 1 
ATOM   5010 C CD2 . TRP   B 1 297 ? -28.815 10.780  -17.490 1.00 35.32  ? 294 TRP   B CD2 1 
ATOM   5011 N NE1 . TRP   B 1 297 ? -26.690 10.384  -16.880 1.00 31.90  ? 294 TRP   B NE1 1 
ATOM   5012 C CE2 . TRP   B 1 297 ? -27.926 10.719  -16.392 1.00 35.38  ? 294 TRP   B CE2 1 
ATOM   5013 C CE3 . TRP   B 1 297 ? -30.153 11.094  -17.254 1.00 34.36  ? 294 TRP   B CE3 1 
ATOM   5014 C CZ2 . TRP   B 1 297 ? -28.340 10.958  -15.078 1.00 33.91  ? 294 TRP   B CZ2 1 
ATOM   5015 C CZ3 . TRP   B 1 297 ? -30.559 11.335  -15.951 1.00 35.90  ? 294 TRP   B CZ3 1 
ATOM   5016 C CH2 . TRP   B 1 297 ? -29.656 11.268  -14.877 1.00 32.85  ? 294 TRP   B CH2 1 
ATOM   5017 N N   . PHE   B 1 298 ? -28.087 11.772  -23.294 1.00 46.80  ? 295 PHE   B N   1 
ATOM   5018 C CA  . PHE   B 1 298 ? -28.555 11.683  -24.678 1.00 43.78  ? 295 PHE   B CA  1 
ATOM   5019 C C   . PHE   B 1 298 ? -27.442 11.040  -25.505 1.00 40.71  ? 295 PHE   B C   1 
ATOM   5020 O O   . PHE   B 1 298 ? -26.715 11.685  -26.262 1.00 39.65  ? 295 PHE   B O   1 
ATOM   5021 C CB  . PHE   B 1 298 ? -28.960 13.057  -25.214 1.00 39.29  ? 295 PHE   B CB  1 
ATOM   5022 C CG  . PHE   B 1 298 ? -30.304 13.564  -24.674 1.00 37.70  ? 295 PHE   B CG  1 
ATOM   5023 C CD1 . PHE   B 1 298 ? -30.679 13.339  -23.363 1.00 36.96  ? 295 PHE   B CD1 1 
ATOM   5024 C CD2 . PHE   B 1 298 ? -31.175 14.281  -25.488 1.00 40.66  ? 295 PHE   B CD2 1 
ATOM   5025 C CE1 . PHE   B 1 298 ? -31.908 13.803  -22.873 1.00 40.88  ? 295 PHE   B CE1 1 
ATOM   5026 C CE2 . PHE   B 1 298 ? -32.401 14.752  -25.008 1.00 39.66  ? 295 PHE   B CE2 1 
ATOM   5027 C CZ  . PHE   B 1 298 ? -32.766 14.509  -23.695 1.00 39.24  ? 295 PHE   B CZ  1 
ATOM   5028 N N   . THR   B 1 299 ? -27.298 9.728   -25.342 1.00 44.34  ? 296 THR   B N   1 
ATOM   5029 C CA  . THR   B 1 299 ? -26.289 8.952   -26.048 1.00 45.77  ? 296 THR   B CA  1 
ATOM   5030 C C   . THR   B 1 299 ? -26.993 7.813   -26.768 1.00 50.01  ? 296 THR   B C   1 
ATOM   5031 O O   . THR   B 1 299 ? -28.047 7.335   -26.318 1.00 47.27  ? 296 THR   B O   1 
ATOM   5032 C CB  . THR   B 1 299 ? -25.198 8.400   -25.075 1.00 51.15  ? 296 THR   B CB  1 
ATOM   5033 O OG1 . THR   B 1 299 ? -25.681 7.237   -24.377 1.00 46.57  ? 296 THR   B OG1 1 
ATOM   5034 C CG2 . THR   B 1 299 ? -24.811 9.451   -24.036 1.00 46.46  ? 296 THR   B CG2 1 
ATOM   5035 N N   . GLU   B 1 300 ? -26.411 7.392   -27.901 1.00 51.49  ? 297 GLU   B N   1 
ATOM   5036 C CA  . GLU   B 1 300 ? -26.997 6.289   -28.664 1.00 54.09  ? 297 GLU   B CA  1 
ATOM   5037 C C   . GLU   B 1 300 ? -27.235 5.064   -27.781 1.00 55.96  ? 297 GLU   B C   1 
ATOM   5038 O O   . GLU   B 1 300 ? -28.342 4.511   -27.748 1.00 56.27  ? 297 GLU   B O   1 
ATOM   5039 C CB  . GLU   B 1 300 ? -26.117 5.914   -29.860 1.00 57.50  ? 297 GLU   B CB  1 
ATOM   5040 C CG  . GLU   B 1 300 ? -26.551 4.589   -30.510 1.00 62.55  ? 297 GLU   B CG  1 
ATOM   5041 C CD  . GLU   B 1 300 ? -25.826 4.258   -31.822 1.00 72.63  ? 297 GLU   B CD  1 
ATOM   5042 O OE1 . GLU   B 1 300 ? -24.923 5.022   -32.238 1.00 70.96  ? 297 GLU   B OE1 1 
ATOM   5043 O OE2 . GLU   B 1 300 ? -26.178 3.226   -32.445 1.00 70.86  ? 297 GLU   B OE2 1 
ATOM   5044 N N   . GLN   B 1 301 ? -26.211 4.639   -27.035 1.00 55.84  ? 298 GLN   B N   1 
ATOM   5045 C CA  . GLN   B 1 301 ? -26.387 3.448   -26.216 1.00 56.52  ? 298 GLN   B CA  1 
ATOM   5046 C C   . GLN   B 1 301 ? -27.465 3.658   -25.169 1.00 55.63  ? 298 GLN   B C   1 
ATOM   5047 O O   . GLN   B 1 301 ? -28.204 2.720   -24.851 1.00 60.67  ? 298 GLN   B O   1 
ATOM   5048 C CB  . GLN   B 1 301 ? -25.074 3.030   -25.552 1.00 57.02  ? 298 GLN   B CB  1 
ATOM   5049 C CG  . GLN   B 1 301 ? -24.972 1.511   -25.326 1.00 73.30  ? 298 GLN   B CG  1 
ATOM   5050 C CD  . GLN   B 1 301 ? -23.834 1.097   -24.383 1.00 87.02  ? 298 GLN   B CD  1 
ATOM   5051 O OE1 . GLN   B 1 301 ? -23.175 1.946   -23.774 1.00 84.65  ? 298 GLN   B OE1 1 
ATOM   5052 N NE2 . GLN   B 1 301 ? -23.608 -0.215  -24.257 1.00 79.29  ? 298 GLN   B NE2 1 
ATOM   5053 N N   . ASN   B 1 302 ? -27.599 4.879   -24.641 1.00 52.23  ? 299 ASN   B N   1 
ATOM   5054 C CA  . ASN   B 1 302 ? -28.602 5.094   -23.601 1.00 51.04  ? 299 ASN   B CA  1 
ATOM   5055 C C   . ASN   B 1 302 ? -30.017 5.077   -24.164 1.00 54.91  ? 299 ASN   B C   1 
ATOM   5056 O O   . ASN   B 1 302 ? -30.954 4.658   -23.468 1.00 50.56  ? 299 ASN   B O   1 
ATOM   5057 C CB  . ASN   B 1 302 ? -28.348 6.405   -22.863 1.00 45.93  ? 299 ASN   B CB  1 
ATOM   5058 C CG  . ASN   B 1 302 ? -27.425 6.237   -21.674 1.00 53.95  ? 299 ASN   B CG  1 
ATOM   5059 O OD1 . ASN   B 1 302 ? -27.779 5.588   -20.685 1.00 53.85  ? 299 ASN   B OD1 1 
ATOM   5060 N ND2 . ASN   B 1 302 ? -26.238 6.836   -21.755 1.00 52.92  ? 299 ASN   B ND2 1 
ATOM   5061 N N   . TRP   B 1 303 ? -30.203 5.527   -25.410 1.00 52.21  ? 300 TRP   B N   1 
ATOM   5062 C CA  . TRP   B 1 303 ? -31.535 5.456   -26.003 1.00 53.10  ? 300 TRP   B CA  1 
ATOM   5063 C C   . TRP   B 1 303 ? -31.967 4.003   -26.185 1.00 53.36  ? 300 TRP   B C   1 
ATOM   5064 O O   . TRP   B 1 303 ? -33.051 3.611   -25.729 1.00 52.08  ? 300 TRP   B O   1 
ATOM   5065 C CB  . TRP   B 1 303 ? -31.573 6.229   -27.325 1.00 51.72  ? 300 TRP   B CB  1 
ATOM   5066 C CG  . TRP   B 1 303 ? -31.505 7.737   -27.152 1.00 46.79  ? 300 TRP   B CG  1 
ATOM   5067 C CD1 . TRP   B 1 303 ? -30.523 8.563   -27.597 1.00 46.32  ? 300 TRP   B CD1 1 
ATOM   5068 C CD2 . TRP   B 1 303 ? -32.453 8.578   -26.469 1.00 44.15  ? 300 TRP   B CD2 1 
ATOM   5069 N NE1 . TRP   B 1 303 ? -30.802 9.864   -27.253 1.00 43.46  ? 300 TRP   B NE1 1 
ATOM   5070 C CE2 . TRP   B 1 303 ? -31.979 9.896   -26.550 1.00 43.93  ? 300 TRP   B CE2 1 
ATOM   5071 C CE3 . TRP   B 1 303 ? -33.653 8.340   -25.800 1.00 43.20  ? 300 TRP   B CE3 1 
ATOM   5072 C CZ2 . TRP   B 1 303 ? -32.664 10.969  -25.992 1.00 38.87  ? 300 TRP   B CZ2 1 
ATOM   5073 C CZ3 . TRP   B 1 303 ? -34.327 9.402   -25.247 1.00 39.35  ? 300 TRP   B CZ3 1 
ATOM   5074 C CH2 . TRP   B 1 303 ? -33.832 10.699  -25.343 1.00 42.22  ? 300 TRP   B CH2 1 
ATOM   5075 N N   . SER   B 1 304 ? -31.106 3.186   -26.818 1.00 49.02  ? 301 SER   B N   1 
ATOM   5076 C CA  . SER   B 1 304 ? -31.337 1.744   -26.934 1.00 49.67  ? 301 SER   B CA  1 
ATOM   5077 C C   . SER   B 1 304 ? -31.775 1.147   -25.608 1.00 55.03  ? 301 SER   B C   1 
ATOM   5078 O O   . SER   B 1 304 ? -32.758 0.399   -25.539 1.00 60.49  ? 301 SER   B O   1 
ATOM   5079 C CB  . SER   B 1 304 ? -30.069 1.022   -27.404 1.00 52.20  ? 301 SER   B CB  1 
ATOM   5080 O OG  . SER   B 1 304 ? -29.639 1.426   -28.688 1.00 52.97  ? 301 SER   B OG  1 
ATOM   5081 N N   . ALA   B 1 305 ? -31.030 1.452   -24.544 1.00 55.05  ? 302 ALA   B N   1 
ATOM   5082 C CA  . ALA   B 1 305 ? -31.366 0.924   -23.228 1.00 55.03  ? 302 ALA   B CA  1 
ATOM   5083 C C   . ALA   B 1 305 ? -32.739 1.411   -22.774 1.00 56.49  ? 302 ALA   B C   1 
ATOM   5084 O O   . ALA   B 1 305 ? -33.521 0.635   -22.210 1.00 57.93  ? 302 ALA   B O   1 
ATOM   5085 C CB  . ALA   B 1 305 ? -30.284 1.305   -22.222 1.00 46.60  ? 302 ALA   B CB  1 
ATOM   5086 N N   . LEU   B 1 306 ? -33.059 2.689   -23.024 1.00 56.66  ? 303 LEU   B N   1 
ATOM   5087 C CA  . LEU   B 1 306 ? -34.367 3.207   -22.626 1.00 56.09  ? 303 LEU   B CA  1 
ATOM   5088 C C   . LEU   B 1 306 ? -35.493 2.477   -23.355 1.00 59.82  ? 303 LEU   B C   1 
ATOM   5089 O O   . LEU   B 1 306 ? -36.528 2.155   -22.752 1.00 58.23  ? 303 LEU   B O   1 
ATOM   5090 C CB  . LEU   B 1 306 ? -34.438 4.712   -22.886 1.00 52.55  ? 303 LEU   B CB  1 
ATOM   5091 C CG  . LEU   B 1 306 ? -35.718 5.470   -22.509 1.00 49.07  ? 303 LEU   B CG  1 
ATOM   5092 C CD1 . LEU   B 1 306 ? -36.053 5.394   -21.016 1.00 44.44  ? 303 LEU   B CD1 1 
ATOM   5093 C CD2 . LEU   B 1 306 ? -35.614 6.921   -22.957 1.00 48.81  ? 303 LEU   B CD2 1 
ATOM   5094 N N   . HIS   B 1 307 ? -35.303 2.163   -24.615 1.00 54.12  ? 304 HIS   B N   1 
ATOM   5095 C CA  . HIS   B 1 307 ? -36.331 1.425   -25.310 1.00 63.65  ? 304 HIS   B CA  1 
ATOM   5096 C C   . HIS   B 1 307 ? -36.495 0.048   -24.701 1.00 63.31  ? 304 HIS   B C   1 
ATOM   5097 O O   . HIS   B 1 307 ? -37.550 -0.282  -24.199 1.00 63.75  ? 304 HIS   B O   1 
ATOM   5098 C CB  . HIS   B 1 307 ? -36.019 1.339   -26.801 1.00 58.28  ? 304 HIS   B CB  1 
ATOM   5099 C CG  . HIS   B 1 307 ? -36.094 2.658   -27.502 1.00 71.83  ? 304 HIS   B CG  1 
ATOM   5100 N ND1 . HIS   B 1 307 ? -37.191 3.486   -27.411 1.00 75.32  ? 304 HIS   B ND1 1 
ATOM   5101 C CD2 . HIS   B 1 307 ? -35.204 3.299   -28.295 1.00 73.94  ? 304 HIS   B CD2 1 
ATOM   5102 C CE1 . HIS   B 1 307 ? -36.977 4.578   -28.123 1.00 70.34  ? 304 HIS   B CE1 1 
ATOM   5103 N NE2 . HIS   B 1 307 ? -35.778 4.489   -28.669 1.00 72.78  ? 304 HIS   B NE2 1 
ATOM   5104 N N   . GLU   B 1 308 ? -35.441 -0.745  -24.720 1.00 63.58  ? 305 GLU   B N   1 
ATOM   5105 C CA  . GLU   B 1 308 ? -35.491 -2.078  -24.123 1.00 59.57  ? 305 GLU   B CA  1 
ATOM   5106 C C   . GLU   B 1 308 ? -36.154 -2.071  -22.751 1.00 63.02  ? 305 GLU   B C   1 
ATOM   5107 O O   . GLU   B 1 308 ? -37.122 -2.800  -22.504 1.00 67.61  ? 305 GLU   B O   1 
ATOM   5108 C CB  . GLU   B 1 308 ? -34.077 -2.643  -24.006 1.00 64.66  ? 305 GLU   B CB  1 
ATOM   5109 C CG  . GLU   B 1 308 ? -33.404 -2.933  -25.320 1.00 74.64  ? 305 GLU   B CG  1 
ATOM   5110 C CD  . GLU   B 1 308 ? -33.329 -4.421  -25.609 1.00 84.89  ? 305 GLU   B CD  1 
ATOM   5111 O OE1 . GLU   B 1 308 ? -33.864 -5.210  -24.795 1.00 80.89  ? 305 GLU   B OE1 1 
ATOM   5112 O OE2 . GLU   B 1 308 ? -32.735 -4.798  -26.646 1.00 92.87  ? 305 GLU   B OE2 1 
ATOM   5113 N N   . GLU   B 1 309 ? -35.634 -1.263  -21.833 1.00 62.25  ? 306 GLU   B N   1 
ATOM   5114 C CA  . GLU   B 1 309 ? -36.107 -1.355  -20.456 1.00 67.48  ? 306 GLU   B CA  1 
ATOM   5115 C C   . GLU   B 1 309 ? -37.510 -0.784  -20.312 1.00 64.76  ? 306 GLU   B C   1 
ATOM   5116 O O   . GLU   B 1 309 ? -38.388 -1.420  -19.718 1.00 71.35  ? 306 GLU   B O   1 
ATOM   5117 C CB  . GLU   B 1 309 ? -35.136 -0.655  -19.507 1.00 62.23  ? 306 GLU   B CB  1 
ATOM   5118 C CG  . GLU   B 1 309 ? -33.827 -1.407  -19.333 1.00 60.09  ? 306 GLU   B CG  1 
ATOM   5119 C CD  . GLU   B 1 309 ? -32.972 -0.820  -18.233 1.00 58.04  ? 306 GLU   B CD  1 
ATOM   5120 O OE1 . GLU   B 1 309 ? -33.527 -0.508  -17.147 1.00 55.87  ? 306 GLU   B OE1 1 
ATOM   5121 O OE2 . GLU   B 1 309 ? -31.752 -0.660  -18.466 1.00 51.79  ? 306 GLU   B OE2 1 
ATOM   5122 N N   . LEU   B 1 310 ? -37.748 0.413   -20.847 1.00 67.55  ? 307 LEU   B N   1 
ATOM   5123 C CA  . LEU   B 1 310 ? -39.043 1.049   -20.644 1.00 66.03  ? 307 LEU   B CA  1 
ATOM   5124 C C   . LEU   B 1 310 ? -40.068 0.661   -21.695 1.00 66.64  ? 307 LEU   B C   1 
ATOM   5125 O O   . LEU   B 1 310 ? -41.268 0.637   -21.387 1.00 63.60  ? 307 LEU   B O   1 
ATOM   5126 C CB  . LEU   B 1 310 ? -38.899 2.572   -20.622 1.00 63.02  ? 307 LEU   B CB  1 
ATOM   5127 C CG  . LEU   B 1 310 ? -38.507 3.185   -19.285 1.00 59.96  ? 307 LEU   B CG  1 
ATOM   5128 C CD1 . LEU   B 1 310 ? -39.019 4.609   -19.197 1.00 60.11  ? 307 LEU   B CD1 1 
ATOM   5129 C CD2 . LEU   B 1 310 ? -39.037 2.342   -18.146 1.00 61.63  ? 307 LEU   B CD2 1 
ATOM   5130 N N   . GLY   B 1 311 ? -39.619 0.349   -22.918 1.00 66.02  ? 308 GLY   B N   1 
ATOM   5131 C CA  . GLY   B 1 311 ? -40.559 0.076   -23.997 1.00 68.97  ? 308 GLY   B CA  1 
ATOM   5132 C C   . GLY   B 1 311 ? -41.508 -1.057  -23.668 1.00 74.21  ? 308 GLY   B C   1 
ATOM   5133 O O   . GLY   B 1 311 ? -42.728 -0.926  -23.816 1.00 70.75  ? 308 GLY   B O   1 
ATOM   5134 N N   . GLY   B 1 312 ? -40.960 -2.178  -23.195 1.00 75.64  ? 309 GLY   B N   1 
ATOM   5135 C CA  . GLY   B 1 312 ? -41.766 -3.312  -22.793 1.00 74.86  ? 309 GLY   B CA  1 
ATOM   5136 C C   . GLY   B 1 312 ? -42.833 -2.957  -21.776 1.00 78.59  ? 309 GLY   B C   1 
ATOM   5137 O O   . GLY   B 1 312 ? -44.036 -3.064  -22.056 1.00 75.35  ? 309 GLY   B O   1 
ATOM   5138 N N   . LEU   B 1 313 ? -42.396 -2.506  -20.597 1.00 73.95  ? 310 LEU   B N   1 
ATOM   5139 C CA  . LEU   B 1 313 ? -43.333 -2.236  -19.511 1.00 74.07  ? 310 LEU   B CA  1 
ATOM   5140 C C   . LEU   B 1 313 ? -44.422 -1.269  -19.934 1.00 73.45  ? 310 LEU   B C   1 
ATOM   5141 O O   . LEU   B 1 313 ? -45.576 -1.408  -19.513 1.00 75.62  ? 310 LEU   B O   1 
ATOM   5142 C CB  . LEU   B 1 313 ? -42.577 -1.683  -18.305 1.00 79.16  ? 310 LEU   B CB  1 
ATOM   5143 C CG  . LEU   B 1 313 ? -41.332 -2.501  -17.966 1.00 74.41  ? 310 LEU   B CG  1 
ATOM   5144 C CD1 . LEU   B 1 313 ? -40.331 -1.647  -17.221 1.00 66.44  ? 310 LEU   B CD1 1 
ATOM   5145 C CD2 . LEU   B 1 313 ? -41.734 -3.734  -17.157 1.00 73.01  ? 310 LEU   B CD2 1 
ATOM   5146 N N   . VAL   B 1 314 ? -44.081 -0.300  -20.781 1.00 74.49  ? 311 VAL   B N   1 
ATOM   5147 C CA  . VAL   B 1 314 ? -45.046 0.719   -21.175 1.00 76.76  ? 311 VAL   B CA  1 
ATOM   5148 C C   . VAL   B 1 314 ? -46.145 0.115   -22.039 1.00 80.18  ? 311 VAL   B C   1 
ATOM   5149 O O   . VAL   B 1 314 ? -47.339 0.354   -21.807 1.00 77.55  ? 311 VAL   B O   1 
ATOM   5150 C CB  . VAL   B 1 314 ? -44.340 1.870   -21.905 1.00 74.81  ? 311 VAL   B CB  1 
ATOM   5151 C CG1 . VAL   B 1 314 ? -45.367 2.696   -22.655 1.00 71.74  ? 311 VAL   B CG1 1 
ATOM   5152 C CG2 . VAL   B 1 314 ? -43.566 2.731   -20.915 1.00 67.73  ? 311 VAL   B CG2 1 
ATOM   5153 N N   . ARG   B 1 315 ? -45.751 -0.665  -23.056 1.00 80.22  ? 312 ARG   B N   1 
ATOM   5154 C CA  . ARG   B 1 315 ? -46.719 -1.242  -23.988 1.00 80.19  ? 312 ARG   B CA  1 
ATOM   5155 C C   . ARG   B 1 315 ? -47.680 -2.191  -23.283 1.00 80.86  ? 312 ARG   B C   1 
ATOM   5156 O O   . ARG   B 1 315 ? -48.888 -2.162  -23.546 1.00 78.29  ? 312 ARG   B O   1 
ATOM   5157 C CB  . ARG   B 1 315 ? -45.991 -1.962  -25.124 1.00 83.89  ? 312 ARG   B CB  1 
ATOM   5158 C CG  . ARG   B 1 315 ? -45.330 -1.020  -26.129 1.00 82.88  ? 312 ARG   B CG  1 
ATOM   5159 C CD  . ARG   B 1 315 ? -45.066 -1.706  -27.470 1.00 84.46  ? 312 ARG   B CD  1 
ATOM   5160 N NE  . ARG   B 1 315 ? -44.039 -2.728  -27.317 1.00 92.70  ? 312 ARG   B NE  1 
ATOM   5161 C CZ  . ARG   B 1 315 ? -42.737 -2.507  -27.442 1.00 88.96  ? 312 ARG   B CZ  1 
ATOM   5162 N NH1 . ARG   B 1 315 ? -42.270 -1.326  -27.825 1.00 81.59  ? 312 ARG   B NH1 1 
ATOM   5163 N NH2 . ARG   B 1 315 ? -41.883 -3.492  -27.169 1.00 82.76  ? 312 ARG   B NH2 1 
ATOM   5164 N N   . ARG   B 1 316 ? -47.162 -3.035  -22.376 1.00 83.61  ? 313 ARG   B N   1 
ATOM   5165 C CA  . ARG   B 1 316 ? -48.004 -3.931  -21.582 1.00 80.23  ? 313 ARG   B CA  1 
ATOM   5166 C C   . ARG   B 1 316 ? -48.966 -3.184  -20.666 1.00 79.21  ? 313 ARG   B C   1 
ATOM   5167 O O   . ARG   B 1 316 ? -49.903 -3.805  -20.148 1.00 80.07  ? 313 ARG   B O   1 
ATOM   5168 C CB  . ARG   B 1 316 ? -47.144 -4.866  -20.724 1.00 74.39  ? 313 ARG   B CB  1 
ATOM   5169 C CG  . ARG   B 1 316 ? -46.038 -5.607  -21.447 1.00 73.43  ? 313 ARG   B CG  1 
ATOM   5170 C CD  . ARG   B 1 316 ? -45.264 -6.449  -20.452 1.00 69.97  ? 313 ARG   B CD  1 
ATOM   5171 N NE  . ARG   B 1 316 ? -43.825 -6.424  -20.691 1.00 77.45  ? 313 ARG   B NE  1 
ATOM   5172 C CZ  . ARG   B 1 316 ? -42.906 -6.598  -19.745 1.00 82.37  ? 313 ARG   B CZ  1 
ATOM   5173 N NH1 . ARG   B 1 316 ? -43.243 -6.813  -18.482 1.00 76.00  ? 313 ARG   B NH1 1 
ATOM   5174 N NH2 . ARG   B 1 316 ? -41.615 -6.547  -20.073 1.00 79.24  ? 313 ARG   B NH2 1 
ATOM   5175 N N   . GLN   B 1 317 ? -48.756 -1.878  -20.463 1.00 80.92  ? 314 GLN   B N   1 
ATOM   5176 C CA  . GLN   B 1 317 ? -49.504 -1.021  -19.542 1.00 80.77  ? 314 GLN   B CA  1 
ATOM   5177 C C   . GLN   B 1 317 ? -49.229 -1.351  -18.076 1.00 81.98  ? 314 GLN   B C   1 
ATOM   5178 O O   . GLN   B 1 317 ? -50.011 -0.966  -17.191 1.00 78.62  ? 314 GLN   B O   1 
ATOM   5179 C CB  . GLN   B 1 317 ? -51.012 -1.054  -19.828 1.00 84.26  ? 314 GLN   B CB  1 
ATOM   5180 C CG  . GLN   B 1 317 ? -51.354 -1.050  -21.318 1.00 82.30  ? 314 GLN   B CG  1 
ATOM   5181 C CD  . GLN   B 1 317 ? -52.541 -0.174  -21.656 1.00 88.52  ? 314 GLN   B CD  1 
ATOM   5182 O OE1 . GLN   B 1 317 ? -52.893 0.741   -20.902 1.00 88.18  ? 314 GLN   B OE1 1 
ATOM   5183 N NE2 . GLN   B 1 317 ? -53.166 -0.444  -22.802 1.00 83.66  ? 314 GLN   B NE2 1 
ATOM   5184 N N   . GLU   B 1 318 ? -48.127 -2.066  -17.808 1.00 81.36  ? 315 GLU   B N   1 
ATOM   5185 C CA  . GLU   B 1 318 ? -47.533 -2.160  -16.475 1.00 76.11  ? 315 GLU   B CA  1 
ATOM   5186 C C   . GLU   B 1 318 ? -47.140 -0.770  -15.990 1.00 79.96  ? 315 GLU   B C   1 
ATOM   5187 O O   . GLU   B 1 318 ? -47.704 -0.249  -15.018 1.00 76.84  ? 315 GLU   B O   1 
ATOM   5188 C CB  . GLU   B 1 318 ? -46.285 -3.051  -16.489 1.00 78.62  ? 315 GLU   B CB  1 
ATOM   5189 C CG  . GLU   B 1 318 ? -46.529 -4.516  -16.770 1.00 80.84  ? 315 GLU   B CG  1 
ATOM   5190 C CD  . GLU   B 1 318 ? -45.243 -5.321  -16.840 1.00 85.53  ? 315 GLU   B CD  1 
ATOM   5191 O OE1 . GLU   B 1 318 ? -44.150 -4.706  -16.857 1.00 88.69  ? 315 GLU   B OE1 1 
ATOM   5192 O OE2 . GLU   B 1 318 ? -45.330 -6.569  -16.877 1.00 84.56  ? 315 GLU   B OE2 1 
ATOM   5193 N N   . LEU   B 1 319 ? -46.182 -0.178  -16.722 1.00 75.68  ? 316 LEU   B N   1 
ATOM   5194 C CA  . LEU   B 1 319 ? -45.763 1.187   -16.466 1.00 71.89  ? 316 LEU   B CA  1 
ATOM   5195 C C   . LEU   B 1 319 ? -46.631 2.064   -17.328 1.00 68.84  ? 316 LEU   B C   1 
ATOM   5196 O O   . LEU   B 1 319 ? -46.711 1.852   -18.522 1.00 70.68  ? 316 LEU   B O   1 
ATOM   5197 C CB  . LEU   B 1 319 ? -44.307 1.363   -16.837 1.00 74.57  ? 316 LEU   B CB  1 
ATOM   5198 C CG  . LEU   B 1 319 ? -43.574 2.635   -16.432 1.00 67.58  ? 316 LEU   B CG  1 
ATOM   5199 C CD1 . LEU   B 1 319 ? -42.936 2.452   -15.067 1.00 60.05  ? 316 LEU   B CD1 1 
ATOM   5200 C CD2 . LEU   B 1 319 ? -42.510 2.920   -17.473 1.00 70.74  ? 316 LEU   B CD2 1 
ATOM   5201 N N   . VAL   B 1 320 ? -47.239 3.075   -16.750 1.00 65.62  ? 317 VAL   B N   1 
ATOM   5202 C CA  . VAL   B 1 320 ? -48.217 3.913   -17.444 1.00 65.76  ? 317 VAL   B CA  1 
ATOM   5203 C C   . VAL   B 1 320 ? -47.561 5.220   -17.880 1.00 72.37  ? 317 VAL   B C   1 
ATOM   5204 O O   . VAL   B 1 320 ? -47.089 5.994   -17.040 1.00 72.31  ? 317 VAL   B O   1 
ATOM   5205 C CB  . VAL   B 1 320 ? -49.433 4.190   -16.549 1.00 67.21  ? 317 VAL   B CB  1 
ATOM   5206 C CG1 . VAL   B 1 320 ? -50.168 5.441   -17.009 1.00 66.84  ? 317 VAL   B CG1 1 
ATOM   5207 C CG2 . VAL   B 1 320 ? -50.370 2.993   -16.545 1.00 70.30  ? 317 VAL   B CG2 1 
ATOM   5208 N N   . ALA   B 1 321 ? -47.565 5.480   -19.191 1.00 72.16  ? 318 ALA   B N   1 
ATOM   5209 C CA  . ALA   B 1 321 ? -46.968 6.674   -19.802 1.00 67.37  ? 318 ALA   B CA  1 
ATOM   5210 C C   . ALA   B 1 321 ? -48.033 7.408   -20.621 1.00 69.27  ? 318 ALA   B C   1 
ATOM   5211 O O   . ALA   B 1 321 ? -48.191 7.174   -21.823 1.00 61.42  ? 318 ALA   B O   1 
ATOM   5212 C CB  . ALA   B 1 321 ? -45.753 6.300   -20.674 1.00 63.27  ? 318 ALA   B CB  1 
ATOM   5213 N N   . HIS   B 1 322 ? -48.749 8.316   -19.967 1.00 67.26  ? 319 HIS   B N   1 
ATOM   5214 C CA  . HIS   B 1 322 ? -49.830 9.053   -20.598 1.00 61.84  ? 319 HIS   B CA  1 
ATOM   5215 C C   . HIS   B 1 322 ? -49.309 10.263  -21.376 1.00 63.65  ? 319 HIS   B C   1 
ATOM   5216 O O   . HIS   B 1 322 ? -48.214 10.774  -21.132 1.00 63.39  ? 319 HIS   B O   1 
ATOM   5217 C CB  . HIS   B 1 322 ? -50.831 9.502   -19.536 1.00 58.49  ? 319 HIS   B CB  1 
ATOM   5218 C CG  . HIS   B 1 322 ? -51.691 8.391   -19.023 1.00 69.98  ? 319 HIS   B CG  1 
ATOM   5219 N ND1 . HIS   B 1 322 ? -52.409 8.484   -17.848 1.00 69.70  ? 319 HIS   B ND1 1 
ATOM   5220 C CD2 . HIS   B 1 322 ? -51.956 7.164   -19.532 1.00 61.68  ? 319 HIS   B CD2 1 
ATOM   5221 C CE1 . HIS   B 1 322 ? -53.078 7.361   -17.656 1.00 69.01  ? 319 HIS   B CE1 1 
ATOM   5222 N NE2 . HIS   B 1 322 ? -52.819 6.544   -18.663 1.00 66.95  ? 319 HIS   B NE2 1 
ATOM   5223 N N   . GLU   B 1 323 ? -50.122 10.729  -22.321 1.00 61.40  ? 320 GLU   B N   1 
ATOM   5224 C CA  . GLU   B 1 323 ? -49.841 11.965  -23.037 1.00 56.54  ? 320 GLU   B CA  1 
ATOM   5225 C C   . GLU   B 1 323 ? -51.133 12.720  -23.297 1.00 53.22  ? 320 GLU   B C   1 
ATOM   5226 O O   . GLU   B 1 323 ? -52.207 12.128  -23.406 1.00 58.69  ? 320 GLU   B O   1 
ATOM   5227 C CB  . GLU   B 1 323 ? -49.120 11.711  -24.360 1.00 50.07  ? 320 GLU   B CB  1 
ATOM   5228 C CG  . GLU   B 1 323 ? -49.929 10.969  -25.383 1.00 49.29  ? 320 GLU   B CG  1 
ATOM   5229 C CD  . GLU   B 1 323 ? -49.071 10.521  -26.565 1.00 60.37  ? 320 GLU   B CD  1 
ATOM   5230 O OE1 . GLU   B 1 323 ? -47.848 10.806  -26.542 1.00 57.60  ? 320 GLU   B OE1 1 
ATOM   5231 O OE2 . GLU   B 1 323 ? -49.611 9.889   -27.516 1.00 60.14  ? 320 GLU   B OE2 1 
ATOM   5232 N N   . THR   B 1 324 ? -51.012 14.039  -23.380 1.00 54.16  ? 321 THR   B N   1 
ATOM   5233 C CA  . THR   B 1 324 ? -52.114 14.950  -23.695 1.00 53.06  ? 321 THR   B CA  1 
ATOM   5234 C C   . THR   B 1 324 ? -51.690 15.724  -24.942 1.00 49.67  ? 321 THR   B C   1 
ATOM   5235 O O   . THR   B 1 324 ? -50.979 16.724  -24.834 1.00 50.90  ? 321 THR   B O   1 
ATOM   5236 C CB  . THR   B 1 324 ? -52.403 15.891  -22.512 1.00 53.17  ? 321 THR   B CB  1 
ATOM   5237 O OG1 . THR   B 1 324 ? -52.783 15.121  -21.366 1.00 55.97  ? 321 THR   B OG1 1 
ATOM   5238 C CG2 . THR   B 1 324 ? -53.498 16.887  -22.848 1.00 48.29  ? 321 THR   B CG2 1 
ATOM   5239 N N   . VAL   B 1 325 ? -52.115 15.261  -26.114 1.00 43.99  ? 322 VAL   B N   1 
ATOM   5240 C CA  . VAL   B 1 325 ? -51.753 15.881  -27.389 1.00 46.31  ? 322 VAL   B CA  1 
ATOM   5241 C C   . VAL   B 1 325 ? -52.836 16.866  -27.815 1.00 47.32  ? 322 VAL   B C   1 
ATOM   5242 O O   . VAL   B 1 325 ? -53.899 16.458  -28.285 1.00 52.26  ? 322 VAL   B O   1 
ATOM   5243 C CB  . VAL   B 1 325 ? -51.553 14.827  -28.477 1.00 44.76  ? 322 VAL   B CB  1 
ATOM   5244 C CG1 . VAL   B 1 325 ? -51.099 15.498  -29.765 1.00 41.96  ? 322 VAL   B CG1 1 
ATOM   5245 C CG2 . VAL   B 1 325 ? -50.575 13.744  -27.993 1.00 48.94  ? 322 VAL   B CG2 1 
ATOM   5246 N N   . GLN   B 1 326 ? -52.554 18.159  -27.694 1.00 50.24  ? 323 GLN   B N   1 
ATOM   5247 C CA  . GLN   B 1 326 ? -53.413 19.190  -28.263 1.00 47.03  ? 323 GLN   B CA  1 
ATOM   5248 C C   . GLN   B 1 326 ? -53.201 19.269  -29.776 1.00 47.61  ? 323 GLN   B C   1 
ATOM   5249 O O   . GLN   B 1 326 ? -52.137 18.911  -30.285 1.00 48.83  ? 323 GLN   B O   1 
ATOM   5250 C CB  . GLN   B 1 326 ? -53.118 20.537  -27.599 1.00 45.36  ? 323 GLN   B CB  1 
ATOM   5251 C CG  . GLN   B 1 326 ? -53.988 21.677  -28.062 1.00 54.41  ? 323 GLN   B CG  1 
ATOM   5252 C CD  . GLN   B 1 326 ? -55.470 21.383  -27.888 1.00 64.36  ? 323 GLN   B CD  1 
ATOM   5253 O OE1 . GLN   B 1 326 ? -56.233 21.333  -28.871 1.00 53.87  ? 323 GLN   B OE1 1 
ATOM   5254 N NE2 . GLN   B 1 326 ? -55.888 21.184  -26.630 1.00 58.81  ? 323 GLN   B NE2 1 
ATOM   5255 N N   . ASP   B 1 327 ? -54.231 19.720  -30.502 1.00 51.52  ? 324 ASP   B N   1 
ATOM   5256 C CA  . ASP   B 1 327 ? -54.186 19.832  -31.961 1.00 48.84  ? 324 ASP   B CA  1 
ATOM   5257 C C   . ASP   B 1 327 ? -54.098 21.291  -32.399 1.00 48.17  ? 324 ASP   B C   1 
ATOM   5258 O O   . ASP   B 1 327 ? -54.791 22.163  -31.858 1.00 45.04  ? 324 ASP   B O   1 
ATOM   5259 C CB  . ASP   B 1 327 ? -55.415 19.189  -32.611 1.00 50.19  ? 324 ASP   B CB  1 
ATOM   5260 C CG  . ASP   B 1 327 ? -55.084 17.911  -33.373 1.00 57.25  ? 324 ASP   B CG  1 
ATOM   5261 O OD1 . ASP   B 1 327 ? -54.028 17.288  -33.118 1.00 58.00  ? 324 ASP   B OD1 1 
ATOM   5262 O OD2 . ASP   B 1 327 ? -55.896 17.525  -34.240 1.00 69.02  ? 324 ASP   B OD2 1 
ATOM   5263 N N   . GLY   B 1 328 ? -53.239 21.557  -33.377 1.00 44.79  ? 325 GLY   B N   1 
ATOM   5264 C CA  . GLY   B 1 328 ? -53.229 22.873  -33.987 1.00 43.26  ? 325 GLY   B CA  1 
ATOM   5265 C C   . GLY   B 1 328 ? -52.101 23.806  -33.596 1.00 41.77  ? 325 GLY   B C   1 
ATOM   5266 O O   . GLY   B 1 328 ? -51.949 24.182  -32.428 1.00 43.88  ? 325 GLY   B O   1 
ATOM   5267 N N   . PHE   B 1 329 ? -51.335 24.221  -34.606 1.00 39.09  ? 326 PHE   B N   1 
ATOM   5268 C CA  . PHE   B 1 329 ? -50.161 25.058  -34.391 1.00 34.26  ? 326 PHE   B CA  1 
ATOM   5269 C C   . PHE   B 1 329 ? -50.498 26.384  -33.713 1.00 32.36  ? 326 PHE   B C   1 
ATOM   5270 O O   . PHE   B 1 329 ? -49.664 26.941  -32.989 1.00 32.45  ? 326 PHE   B O   1 
ATOM   5271 C CB  . PHE   B 1 329 ? -49.466 25.310  -35.733 1.00 35.06  ? 326 PHE   B CB  1 
ATOM   5272 C CG  . PHE   B 1 329 ? -48.240 26.159  -35.616 1.00 34.39  ? 326 PHE   B CG  1 
ATOM   5273 C CD1 . PHE   B 1 329 ? -47.005 25.583  -35.350 1.00 32.21  ? 326 PHE   B CD1 1 
ATOM   5274 C CD2 . PHE   B 1 329 ? -48.324 27.538  -35.742 1.00 32.56  ? 326 PHE   B CD2 1 
ATOM   5275 C CE1 . PHE   B 1 329 ? -45.867 26.366  -35.221 1.00 27.55  ? 326 PHE   B CE1 1 
ATOM   5276 C CE2 . PHE   B 1 329 ? -47.204 28.324  -35.606 1.00 31.75  ? 326 PHE   B CE2 1 
ATOM   5277 C CZ  . PHE   B 1 329 ? -45.970 27.737  -35.352 1.00 30.37  ? 326 PHE   B CZ  1 
ATOM   5278 N N   . GLU   B 1 330 ? -51.688 26.921  -33.952 1.00 37.46  ? 327 GLU   B N   1 
ATOM   5279 C CA  . GLU   B 1 330 ? -52.047 28.207  -33.371 1.00 39.32  ? 327 GLU   B CA  1 
ATOM   5280 C C   . GLU   B 1 330 ? -52.380 28.097  -31.888 1.00 37.29  ? 327 GLU   B C   1 
ATOM   5281 O O   . GLU   B 1 330 ? -52.575 29.125  -31.218 1.00 33.10  ? 327 GLU   B O   1 
ATOM   5282 C CB  . GLU   B 1 330 ? -53.227 28.801  -34.147 1.00 36.75  ? 327 GLU   B CB  1 
ATOM   5283 C CG  . GLU   B 1 330 ? -54.512 27.973  -34.070 1.00 40.73  ? 327 GLU   B CG  1 
ATOM   5284 C CD  . GLU   B 1 330 ? -54.542 26.760  -35.019 1.00 48.15  ? 327 GLU   B CD  1 
ATOM   5285 O OE1 . GLU   B 1 330 ? -53.517 26.415  -35.667 1.00 47.61  ? 327 GLU   B OE1 1 
ATOM   5286 O OE2 . GLU   B 1 330 ? -55.637 26.147  -35.100 1.00 51.69  ? 327 GLU   B OE2 1 
ATOM   5287 N N   . HIS   B 1 331 ? -52.437 26.879  -31.365 1.00 35.19  ? 328 HIS   B N   1 
ATOM   5288 C CA  . HIS   B 1 331 ? -52.793 26.650  -29.978 1.00 38.96  ? 328 HIS   B CA  1 
ATOM   5289 C C   . HIS   B 1 331 ? -51.587 26.339  -29.106 1.00 40.23  ? 328 HIS   B C   1 
ATOM   5290 O O   . HIS   B 1 331 ? -51.753 26.150  -27.893 1.00 42.02  ? 328 HIS   B O   1 
ATOM   5291 C CB  . HIS   B 1 331 ? -53.837 25.526  -29.892 1.00 35.61  ? 328 HIS   B CB  1 
ATOM   5292 C CG  . HIS   B 1 331 ? -55.132 25.871  -30.564 1.00 38.21  ? 328 HIS   B CG  1 
ATOM   5293 N ND1 . HIS   B 1 331 ? -55.854 27.003  -30.244 1.00 38.74  ? 328 HIS   B ND1 1 
ATOM   5294 C CD2 . HIS   B 1 331 ? -55.819 25.254  -31.558 1.00 37.11  ? 328 HIS   B CD2 1 
ATOM   5295 C CE1 . HIS   B 1 331 ? -56.930 27.065  -31.008 1.00 36.60  ? 328 HIS   B CE1 1 
ATOM   5296 N NE2 . HIS   B 1 331 ? -56.931 26.018  -31.815 1.00 36.58  ? 328 HIS   B NE2 1 
ATOM   5297 N N   . ILE   B 1 332 ? -50.376 26.320  -29.685 1.00 38.15  ? 329 ILE   B N   1 
ATOM   5298 C CA  . ILE   B 1 332 ? -49.185 26.013  -28.892 1.00 35.71  ? 329 ILE   B CA  1 
ATOM   5299 C C   . ILE   B 1 332 ? -49.046 26.895  -27.657 1.00 35.34  ? 329 ILE   B C   1 
ATOM   5300 O O   . ILE   B 1 332 ? -48.874 26.349  -26.561 1.00 36.32  ? 329 ILE   B O   1 
ATOM   5301 C CB  . ILE   B 1 332 ? -47.922 26.050  -29.796 1.00 31.11  ? 329 ILE   B CB  1 
ATOM   5302 C CG1 . ILE   B 1 332 ? -47.938 24.864  -30.745 1.00 28.08  ? 329 ILE   B CG1 1 
ATOM   5303 C CG2 . ILE   B 1 332 ? -46.696 26.037  -28.932 1.00 27.64  ? 329 ILE   B CG2 1 
ATOM   5304 C CD1 . ILE   B 1 332 ? -46.887 24.935  -31.801 1.00 29.69  ? 329 ILE   B CD1 1 
ATOM   5305 N N   . PRO   B 1 333 ? -49.142 28.229  -27.740 1.00 37.42  ? 330 PRO   B N   1 
ATOM   5306 C CA  . PRO   B 1 333 ? -48.983 29.011  -26.498 1.00 34.16  ? 330 PRO   B CA  1 
ATOM   5307 C C   . PRO   B 1 333 ? -50.086 28.757  -25.485 1.00 38.12  ? 330 PRO   B C   1 
ATOM   5308 O O   . PRO   B 1 333 ? -49.817 28.821  -24.279 1.00 35.92  ? 330 PRO   B O   1 
ATOM   5309 C CB  . PRO   B 1 333 ? -48.967 30.473  -26.979 1.00 25.53  ? 330 PRO   B CB  1 
ATOM   5310 C CG  . PRO   B 1 333 ? -48.582 30.391  -28.426 1.00 33.36  ? 330 PRO   B CG  1 
ATOM   5311 C CD  . PRO   B 1 333 ? -49.234 29.108  -28.922 1.00 31.51  ? 330 PRO   B CD  1 
ATOM   5312 N N   . ALA   B 1 334 ? -51.315 28.453  -25.918 1.00 36.87  ? 331 ALA   B N   1 
ATOM   5313 C CA  . ALA   B 1 334 ? -52.366 28.193  -24.933 1.00 35.34  ? 331 ALA   B CA  1 
ATOM   5314 C C   . ALA   B 1 334 ? -52.172 26.836  -24.273 1.00 34.86  ? 331 ALA   B C   1 
ATOM   5315 O O   . ALA   B 1 334 ? -52.462 26.673  -23.082 1.00 33.42  ? 331 ALA   B O   1 
ATOM   5316 C CB  . ALA   B 1 334 ? -53.750 28.282  -25.575 1.00 30.17  ? 331 ALA   B CB  1 
ATOM   5317 N N   . ALA   B 1 335 ? -51.708 25.847  -25.041 1.00 34.23  ? 332 ALA   B N   1 
ATOM   5318 C CA  . ALA   B 1 335 ? -51.340 24.562  -24.459 1.00 34.93  ? 332 ALA   B CA  1 
ATOM   5319 C C   . ALA   B 1 335 ? -50.227 24.731  -23.435 1.00 38.49  ? 332 ALA   B C   1 
ATOM   5320 O O   . ALA   B 1 335 ? -50.277 24.171  -22.334 1.00 42.44  ? 332 ALA   B O   1 
ATOM   5321 C CB  . ALA   B 1 335 ? -50.907 23.600  -25.560 1.00 36.21  ? 332 ALA   B CB  1 
ATOM   5322 N N   . TYR   B 1 336 ? -49.205 25.501  -23.789 1.00 39.91  ? 333 TYR   B N   1 
ATOM   5323 C CA  . TYR   B 1 336 ? -48.135 25.806  -22.851 1.00 38.11  ? 333 TYR   B CA  1 
ATOM   5324 C C   . TYR   B 1 336 ? -48.652 26.543  -21.622 1.00 38.37  ? 333 TYR   B C   1 
ATOM   5325 O O   . TYR   B 1 336 ? -48.141 26.335  -20.511 1.00 39.97  ? 333 TYR   B O   1 
ATOM   5326 C CB  . TYR   B 1 336 ? -47.075 26.620  -23.578 1.00 33.04  ? 333 TYR   B CB  1 
ATOM   5327 C CG  . TYR   B 1 336 ? -46.031 27.276  -22.726 1.00 30.23  ? 333 TYR   B CG  1 
ATOM   5328 C CD1 . TYR   B 1 336 ? -44.999 26.534  -22.156 1.00 31.13  ? 333 TYR   B CD1 1 
ATOM   5329 C CD2 . TYR   B 1 336 ? -46.037 28.642  -22.542 1.00 30.32  ? 333 TYR   B CD2 1 
ATOM   5330 C CE1 . TYR   B 1 336 ? -44.020 27.151  -21.398 1.00 33.72  ? 333 TYR   B CE1 1 
ATOM   5331 C CE2 . TYR   B 1 336 ? -45.057 29.271  -21.792 1.00 33.72  ? 333 TYR   B CE2 1 
ATOM   5332 C CZ  . TYR   B 1 336 ? -44.052 28.521  -21.221 1.00 35.00  ? 333 TYR   B CZ  1 
ATOM   5333 O OH  . TYR   B 1 336 ? -43.084 29.153  -20.475 1.00 35.66  ? 333 TYR   B OH  1 
ATOM   5334 N N   . GLN   B 1 337 ? -49.666 27.395  -21.795 1.00 37.42  ? 334 GLN   B N   1 
ATOM   5335 C CA  . GLN   B 1 337 ? -50.187 28.170  -20.671 1.00 38.47  ? 334 GLN   B CA  1 
ATOM   5336 C C   . GLN   B 1 337 ? -50.861 27.272  -19.637 1.00 41.81  ? 334 GLN   B C   1 
ATOM   5337 O O   . GLN   B 1 337 ? -50.853 27.595  -18.439 1.00 41.44  ? 334 GLN   B O   1 
ATOM   5338 C CB  . GLN   B 1 337 ? -51.163 29.235  -21.183 1.00 38.30  ? 334 GLN   B CB  1 
ATOM   5339 C CG  . GLN   B 1 337 ? -51.770 30.133  -20.119 1.00 36.47  ? 334 GLN   B CG  1 
ATOM   5340 C CD  . GLN   B 1 337 ? -50.761 31.048  -19.464 1.00 41.75  ? 334 GLN   B CD  1 
ATOM   5341 O OE1 . GLN   B 1 337 ? -50.363 32.067  -20.030 1.00 44.36  ? 334 GLN   B OE1 1 
ATOM   5342 N NE2 . GLN   B 1 337 ? -50.347 30.698  -18.253 1.00 44.89  ? 334 GLN   B NE2 1 
ATOM   5343 N N   . THR   B 1 338 ? -51.427 26.134  -20.067 1.00 36.19  ? 335 THR   B N   1 
ATOM   5344 C CA  . THR   B 1 338 ? -52.150 25.306  -19.107 1.00 44.77  ? 335 THR   B CA  1 
ATOM   5345 C C   . THR   B 1 338 ? -51.224 24.759  -18.029 1.00 48.53  ? 335 THR   B C   1 
ATOM   5346 O O   . THR   B 1 338 ? -51.657 24.590  -16.884 1.00 49.59  ? 335 THR   B O   1 
ATOM   5347 C CB  . THR   B 1 338 ? -52.893 24.162  -19.805 1.00 45.26  ? 335 THR   B CB  1 
ATOM   5348 O OG1 . THR   B 1 338 ? -51.959 23.269  -20.430 1.00 42.11  ? 335 THR   B OG1 1 
ATOM   5349 C CG2 . THR   B 1 338 ? -53.851 24.713  -20.846 1.00 34.47  ? 335 THR   B CG2 1 
ATOM   5350 N N   . LEU   B 1 339 ? -49.946 24.517  -18.355 1.00 43.01  ? 336 LEU   B N   1 
ATOM   5351 C CA  . LEU   B 1 339 ? -49.025 23.966  -17.366 1.00 39.85  ? 336 LEU   B CA  1 
ATOM   5352 C C   . LEU   B 1 339 ? -48.944 24.841  -16.122 1.00 45.78  ? 336 LEU   B C   1 
ATOM   5353 O O   . LEU   B 1 339 ? -48.611 24.344  -15.040 1.00 44.46  ? 336 LEU   B O   1 
ATOM   5354 C CB  . LEU   B 1 339 ? -47.623 23.788  -17.955 1.00 34.61  ? 336 LEU   B CB  1 
ATOM   5355 C CG  . LEU   B 1 339 ? -47.341 22.994  -19.236 1.00 36.25  ? 336 LEU   B CG  1 
ATOM   5356 C CD1 . LEU   B 1 339 ? -45.878 23.158  -19.644 1.00 31.85  ? 336 LEU   B CD1 1 
ATOM   5357 C CD2 . LEU   B 1 339 ? -47.675 21.534  -19.119 1.00 35.40  ? 336 LEU   B CD2 1 
ATOM   5358 N N   . PHE   B 1 340 ? -49.259 26.127  -16.243 1.00 43.50  ? 337 PHE   B N   1 
ATOM   5359 C CA  . PHE   B 1 340 ? -49.154 27.030  -15.115 1.00 40.72  ? 337 PHE   B CA  1 
ATOM   5360 C C   . PHE   B 1 340 ? -50.499 27.445  -14.550 1.00 46.73  ? 337 PHE   B C   1 
ATOM   5361 O O   . PHE   B 1 340 ? -50.546 27.925  -13.415 1.00 49.05  ? 337 PHE   B O   1 
ATOM   5362 C CB  . PHE   B 1 340 ? -48.377 28.293  -15.519 1.00 40.56  ? 337 PHE   B CB  1 
ATOM   5363 C CG  . PHE   B 1 340 ? -47.049 28.010  -16.193 1.00 47.34  ? 337 PHE   B CG  1 
ATOM   5364 C CD1 . PHE   B 1 340 ? -45.883 27.866  -15.441 1.00 43.00  ? 337 PHE   B CD1 1 
ATOM   5365 C CD2 . PHE   B 1 340 ? -46.961 27.903  -17.588 1.00 45.10  ? 337 PHE   B CD2 1 
ATOM   5366 C CE1 . PHE   B 1 340 ? -44.652 27.611  -16.065 1.00 37.99  ? 337 PHE   B CE1 1 
ATOM   5367 C CE2 . PHE   B 1 340 ? -45.740 27.651  -18.218 1.00 39.21  ? 337 PHE   B CE2 1 
ATOM   5368 C CZ  . PHE   B 1 340 ? -44.584 27.509  -17.452 1.00 41.24  ? 337 PHE   B CZ  1 
ATOM   5369 N N   . SER   B 1 341 ? -51.585 27.275  -15.306 1.00 49.86  ? 338 SER   B N   1 
ATOM   5370 C CA  . SER   B 1 341 ? -52.873 27.877  -14.975 1.00 49.22  ? 338 SER   B CA  1 
ATOM   5371 C C   . SER   B 1 341 ? -54.016 26.875  -14.950 1.00 51.41  ? 338 SER   B C   1 
ATOM   5372 O O   . SER   B 1 341 ? -54.868 26.948  -14.060 1.00 62.15  ? 338 SER   B O   1 
ATOM   5373 C CB  . SER   B 1 341 ? -53.197 28.991  -15.977 1.00 44.46  ? 338 SER   B CB  1 
ATOM   5374 O OG  . SER   B 1 341 ? -52.077 29.825  -16.162 1.00 44.84  ? 338 SER   B OG  1 
ATOM   5375 N N   . ALA   B 1 342 ? -54.045 25.931  -15.888 1.00 49.84  ? 339 ALA   B N   1 
ATOM   5376 C CA  . ALA   B 1 342 ? -55.150 24.996  -16.033 1.00 52.61  ? 339 ALA   B CA  1 
ATOM   5377 C C   . ALA   B 1 342 ? -54.613 23.591  -16.302 1.00 54.65  ? 339 ALA   B C   1 
ATOM   5378 O O   . ALA   B 1 342 ? -54.910 22.962  -17.317 1.00 56.65  ? 339 ALA   B O   1 
ATOM   5379 C CB  . ALA   B 1 342 ? -56.096 25.439  -17.149 1.00 44.35  ? 339 ALA   B CB  1 
ATOM   5380 N N   . SER   B 1 343 ? -53.802 23.078  -15.372 1.00 54.22  ? 340 SER   B N   1 
ATOM   5381 C CA  . SER   B 1 343 ? -53.243 21.735  -15.515 1.00 55.77  ? 340 SER   B CA  1 
ATOM   5382 C C   . SER   B 1 343 ? -54.151 20.651  -14.956 1.00 61.19  ? 340 SER   B C   1 
ATOM   5383 O O   . SER   B 1 343 ? -53.888 19.464  -15.193 1.00 58.91  ? 340 SER   B O   1 
ATOM   5384 C CB  . SER   B 1 343 ? -51.873 21.640  -14.835 1.00 51.98  ? 340 SER   B CB  1 
ATOM   5385 O OG  . SER   B 1 343 ? -51.936 22.017  -13.468 1.00 53.98  ? 340 SER   B OG  1 
ATOM   5386 N N   . GLU   B 1 344 ? -55.215 21.034  -14.274 1.00 64.92  ? 341 GLU   B N   1 
ATOM   5387 C CA  . GLU   B 1 344 ? -56.142 20.080  -13.685 1.00 64.16  ? 341 GLU   B CA  1 
ATOM   5388 C C   . GLU   B 1 344 ? -56.585 19.022  -14.652 1.00 62.96  ? 341 GLU   B C   1 
ATOM   5389 O O   . GLU   B 1 344 ? -56.877 17.910  -14.259 1.00 68.27  ? 341 GLU   B O   1 
ATOM   5390 C CB  . GLU   B 1 344 ? -57.359 20.826  -13.189 1.00 58.68  ? 341 GLU   B CB  1 
ATOM   5391 C CG  . GLU   B 1 344 ? -57.800 21.937  -14.128 1.00 73.09  ? 341 GLU   B CG  1 
ATOM   5392 C CD  . GLU   B 1 344 ? -57.286 23.300  -13.711 1.00 72.07  ? 341 GLU   B CD  1 
ATOM   5393 O OE1 . GLU   B 1 344 ? -56.358 23.361  -12.880 1.00 66.47  ? 341 GLU   B OE1 1 
ATOM   5394 O OE2 . GLU   B 1 344 ? -57.811 24.313  -14.214 1.00 69.83  ? 341 GLU   B OE2 1 
ATOM   5395 N N   . SER   B 1 345 ? -56.634 19.362  -15.919 1.00 59.24  ? 342 SER   B N   1 
ATOM   5396 C CA  . SER   B 1 345 ? -57.103 18.417  -16.922 1.00 62.05  ? 342 SER   B CA  1 
ATOM   5397 C C   . SER   B 1 345 ? -55.982 17.597  -17.558 1.00 62.05  ? 342 SER   B C   1 
ATOM   5398 O O   . SER   B 1 345 ? -56.261 16.540  -18.138 1.00 55.69  ? 342 SER   B O   1 
ATOM   5399 C CB  . SER   B 1 345 ? -57.877 19.166  -18.012 1.00 62.55  ? 342 SER   B CB  1 
ATOM   5400 O OG  . SER   B 1 345 ? -58.374 20.395  -17.500 1.00 73.87  ? 342 SER   B OG  1 
ATOM   5401 N N   . ASN   B 1 346 ? -54.729 18.040  -17.445 1.00 60.79  ? 343 ASN   B N   1 
ATOM   5402 C CA  . ASN   B 1 346 ? -53.637 17.409  -18.180 1.00 54.90  ? 343 ASN   B CA  1 
ATOM   5403 C C   . ASN   B 1 346 ? -53.249 16.065  -17.565 1.00 53.94  ? 343 ASN   B C   1 
ATOM   5404 O O   . ASN   B 1 346 ? -53.442 15.824  -16.371 1.00 51.62  ? 343 ASN   B O   1 
ATOM   5405 C CB  . ASN   B 1 346 ? -52.427 18.338  -18.235 1.00 53.06  ? 343 ASN   B CB  1 
ATOM   5406 C CG  . ASN   B 1 346 ? -52.628 19.498  -19.203 1.00 51.45  ? 343 ASN   B CG  1 
ATOM   5407 O OD1 . ASN   B 1 346 ? -53.191 19.323  -20.288 1.00 53.08  ? 343 ASN   B OD1 1 
ATOM   5408 N ND2 . ASN   B 1 346 ? -52.181 20.686  -18.812 1.00 47.71  ? 343 ASN   B ND2 1 
ATOM   5409 N N   . ARG   B 1 347 ? -52.685 15.214  -18.410 1.00 56.56  ? 344 ARG   B N   1 
ATOM   5410 C CA  . ARG   B 1 347 ? -52.306 13.884  -17.992 1.00 59.92  ? 344 ARG   B CA  1 
ATOM   5411 C C   . ARG   B 1 347 ? -51.033 13.513  -18.701 1.00 53.05  ? 344 ARG   B C   1 
ATOM   5412 O O   . ARG   B 1 347 ? -51.038 13.232  -19.887 1.00 56.91  ? 344 ARG   B O   1 
ATOM   5413 C CB  . ARG   B 1 347 ? -53.425 12.886  -18.309 1.00 55.79  ? 344 ARG   B CB  1 
ATOM   5414 C CG  . ARG   B 1 347 ? -53.984 12.136  -17.117 1.00 56.67  ? 344 ARG   B CG  1 
ATOM   5415 C CD  . ARG   B 1 347 ? -53.754 12.891  -15.827 1.00 60.92  ? 344 ARG   B CD  1 
ATOM   5416 N NE  . ARG   B 1 347 ? -54.891 12.795  -14.923 1.00 68.85  ? 344 ARG   B NE  1 
ATOM   5417 C CZ  . ARG   B 1 347 ? -55.909 13.646  -14.912 1.00 65.51  ? 344 ARG   B CZ  1 
ATOM   5418 N NH1 . ARG   B 1 347 ? -55.936 14.660  -15.764 1.00 62.72  ? 344 ARG   B NH1 1 
ATOM   5419 N NH2 . ARG   B 1 347 ? -56.899 13.484  -14.051 1.00 59.84  ? 344 ARG   B NH2 1 
ATOM   5420 N N   . GLY   B 1 348 ? -49.941 13.498  -17.971 1.00 53.71  ? 345 GLY   B N   1 
ATOM   5421 C CA  . GLY   B 1 348 ? -48.634 13.196  -18.513 1.00 55.85  ? 345 GLY   B CA  1 
ATOM   5422 C C   . GLY   B 1 348 ? -48.064 14.326  -19.340 1.00 52.48  ? 345 GLY   B C   1 
ATOM   5423 O O   . GLY   B 1 348 ? -48.216 15.510  -19.001 1.00 49.28  ? 345 GLY   B O   1 
ATOM   5424 N N   . LYS   B 1 349 ? -47.416 13.938  -20.440 1.00 48.53  ? 346 LYS   B N   1 
ATOM   5425 C CA  . LYS   B 1 349 ? -46.712 14.854  -21.329 1.00 54.20  ? 346 LYS   B CA  1 
ATOM   5426 C C   . LYS   B 1 349 ? -47.709 15.649  -22.170 1.00 51.20  ? 346 LYS   B C   1 
ATOM   5427 O O   . LYS   B 1 349 ? -48.439 15.067  -22.981 1.00 49.02  ? 346 LYS   B O   1 
ATOM   5428 C CB  . LYS   B 1 349 ? -45.770 14.046  -22.232 1.00 54.25  ? 346 LYS   B CB  1 
ATOM   5429 C CG  . LYS   B 1 349 ? -44.689 14.849  -22.957 1.00 48.27  ? 346 LYS   B CG  1 
ATOM   5430 C CD  . LYS   B 1 349 ? -43.695 15.422  -21.961 1.00 50.04  ? 346 LYS   B CD  1 
ATOM   5431 C CE  . LYS   B 1 349 ? -43.021 16.683  -22.488 1.00 48.65  ? 346 LYS   B CE  1 
ATOM   5432 N NZ  . LYS   B 1 349 ? -43.949 17.848  -22.612 1.00 46.66  ? 346 LYS   B NZ  1 
ATOM   5433 N N   . VAL   B 1 350 ? -47.735 16.970  -21.991 1.00 46.08  ? 347 VAL   B N   1 
ATOM   5434 C CA  . VAL   B 1 350 ? -48.496 17.845  -22.882 1.00 45.83  ? 347 VAL   B CA  1 
ATOM   5435 C C   . VAL   B 1 350 ? -47.689 18.096  -24.149 1.00 46.18  ? 347 VAL   B C   1 
ATOM   5436 O O   . VAL   B 1 350 ? -46.586 18.648  -24.091 1.00 51.18  ? 347 VAL   B O   1 
ATOM   5437 C CB  . VAL   B 1 350 ? -48.843 19.174  -22.205 1.00 46.25  ? 347 VAL   B CB  1 
ATOM   5438 C CG1 . VAL   B 1 350 ? -49.708 20.022  -23.155 1.00 38.40  ? 347 VAL   B CG1 1 
ATOM   5439 C CG2 . VAL   B 1 350 ? -49.533 18.932  -20.873 1.00 46.34  ? 347 VAL   B CG2 1 
ATOM   5440 N N   . LEU   B 1 351 ? -48.293 17.785  -25.276 1.00 38.01  ? 348 LEU   B N   1 
ATOM   5441 C CA  . LEU   B 1 351 ? -47.659 18.016  -26.534 1.00 40.43  ? 348 LEU   B CA  1 
ATOM   5442 C C   . LEU   B 1 351 ? -48.649 18.710  -27.433 1.00 44.60  ? 348 LEU   B C   1 
ATOM   5443 O O   . LEU   B 1 351 ? -49.800 18.900  -27.067 1.00 41.26  ? 348 LEU   B O   1 
ATOM   5444 C CB  . LEU   B 1 351 ? -47.249 16.697  -27.146 1.00 40.36  ? 348 LEU   B CB  1 
ATOM   5445 C CG  . LEU   B 1 351 ? -46.277 15.811  -26.377 1.00 46.39  ? 348 LEU   B CG  1 
ATOM   5446 C CD1 . LEU   B 1 351 ? -46.090 14.497  -27.114 1.00 49.38  ? 348 LEU   B CD1 1 
ATOM   5447 C CD2 . LEU   B 1 351 ? -44.948 16.521  -26.206 1.00 48.53  ? 348 LEU   B CD2 1 
ATOM   5448 N N   . VAL   B 1 352 ? -48.205 19.123  -28.606 1.00 38.68  ? 349 VAL   B N   1 
ATOM   5449 C CA  . VAL   B 1 352 ? -49.119 19.708  -29.569 1.00 39.76  ? 349 VAL   B CA  1 
ATOM   5450 C C   . VAL   B 1 352 ? -48.859 19.123  -30.937 1.00 38.14  ? 349 VAL   B C   1 
ATOM   5451 O O   . VAL   B 1 352 ? -47.748 19.172  -31.426 1.00 37.93  ? 349 VAL   B O   1 
ATOM   5452 C CB  . VAL   B 1 352 ? -49.031 21.240  -29.644 1.00 35.48  ? 349 VAL   B CB  1 
ATOM   5453 C CG1 . VAL   B 1 352 ? -50.000 21.764  -30.688 1.00 37.29  ? 349 VAL   B CG1 1 
ATOM   5454 C CG2 . VAL   B 1 352 ? -49.307 21.869  -28.295 1.00 30.61  ? 349 VAL   B CG2 1 
ATOM   5455 N N   . ARG   B 1 353 ? -49.891 18.559  -31.553 1.00 44.09  ? 350 ARG   B N   1 
ATOM   5456 C CA  . ARG   B 1 353 ? -49.759 18.045  -32.904 1.00 41.62  ? 350 ARG   B CA  1 
ATOM   5457 C C   . ARG   B 1 353 ? -49.999 19.148  -33.888 1.00 43.28  ? 350 ARG   B C   1 
ATOM   5458 O O   . ARG   B 1 353 ? -51.005 19.834  -33.817 1.00 46.43  ? 350 ARG   B O   1 
ATOM   5459 C CB  . ARG   B 1 353 ? -50.721 16.904  -33.171 1.00 44.02  ? 350 ARG   B CB  1 
ATOM   5460 C CG  . ARG   B 1 353 ? -50.287 16.002  -34.304 1.00 44.19  ? 350 ARG   B CG  1 
ATOM   5461 C CD  . ARG   B 1 353 ? -51.274 14.873  -34.509 1.00 51.24  ? 350 ARG   B CD  1 
ATOM   5462 N NE  . ARG   B 1 353 ? -51.405 14.546  -35.922 1.00 63.15  ? 350 ARG   B NE  1 
ATOM   5463 C CZ  . ARG   B 1 353 ? -52.345 15.041  -36.715 1.00 62.12  ? 350 ARG   B CZ  1 
ATOM   5464 N NH1 . ARG   B 1 353 ? -53.250 15.877  -36.230 1.00 61.84  ? 350 ARG   B NH1 1 
ATOM   5465 N NH2 . ARG   B 1 353 ? -52.384 14.696  -37.992 1.00 52.74  ? 350 ARG   B NH2 1 
ATOM   5466 N N   . VAL   B 1 354 ? -49.061 19.328  -34.798 1.00 39.94  ? 351 VAL   B N   1 
ATOM   5467 C CA  . VAL   B 1 354 ? -49.149 20.400  -35.743 1.00 42.40  ? 351 VAL   B CA  1 
ATOM   5468 C C   . VAL   B 1 354 ? -49.633 19.872  -37.068 1.00 45.63  ? 351 VAL   B C   1 
ATOM   5469 O O   . VAL   B 1 354 ? -50.612 20.364  -37.604 1.00 48.56  ? 351 VAL   B O   1 
ATOM   5470 C CB  . VAL   B 1 354 ? -47.780 21.057  -35.920 1.00 42.76  ? 351 VAL   B CB  1 
ATOM   5471 C CG1 . VAL   B 1 354 ? -47.774 21.956  -37.138 1.00 40.62  ? 351 VAL   B CG1 1 
ATOM   5472 C CG2 . VAL   B 1 354 ? -47.408 21.832  -34.670 1.00 38.07  ? 351 VAL   B CG2 1 
HETATM 5473 C C8  . A1EBZ C 2 .   ? -18.354 13.743  16.833  1.00 48.37  ? 401 A1EBZ A C8  1 
HETATM 5474 C C5  . A1EBZ C 2 .   ? -13.703 12.170  16.706  1.00 38.69  ? 401 A1EBZ A C5  1 
HETATM 5475 C C6  . A1EBZ C 2 .   ? -16.095 13.004  17.348  1.00 43.88  ? 401 A1EBZ A C6  1 
HETATM 5476 N N1  . A1EBZ C 2 .   ? -23.891 17.300  16.016  1.00 64.03  ? 401 A1EBZ A N1  1 
HETATM 5477 C C2  . A1EBZ C 2 .   ? -14.553 9.794   18.838  1.00 45.96  ? 401 A1EBZ A C2  1 
HETATM 5478 C C4  . A1EBZ C 2 .   ? -15.092 11.821  17.226  1.00 44.79  ? 401 A1EBZ A C4  1 
HETATM 5479 C C21 . A1EBZ C 2 .   ? -21.462 17.537  12.867  1.00 54.26  ? 401 A1EBZ A C21 1 
HETATM 5480 C C23 . A1EBZ C 2 .   ? -19.461 16.247  13.541  1.00 50.70  ? 401 A1EBZ A C23 1 
HETATM 5481 C C24 . A1EBZ C 2 .   ? -18.311 15.898  14.329  1.00 46.80  ? 401 A1EBZ A C24 1 
HETATM 5482 C C25 . A1EBZ C 2 .   ? -17.600 14.789  14.210  1.00 47.00  ? 401 A1EBZ A C25 1 
HETATM 5483 C C27 . A1EBZ C 2 .   ? -18.475 12.633  17.874  1.00 48.41  ? 401 A1EBZ A C27 1 
HETATM 5484 C C29 . A1EBZ C 2 .   ? -16.664 11.203  18.918  1.00 44.24  ? 401 A1EBZ A C29 1 
HETATM 5485 C C1  . A1EBZ C 2 .   ? -14.765 9.253   20.242  1.00 34.52  ? 401 A1EBZ A C1  1 
HETATM 5486 C C10 . A1EBZ C 2 .   ? -19.410 15.987  17.457  1.00 57.68  ? 401 A1EBZ A C10 1 
HETATM 5487 C C11 . A1EBZ C 2 .   ? -20.702 15.857  16.799  1.00 50.79  ? 401 A1EBZ A C11 1 
HETATM 5488 C C12 . A1EBZ C 2 .   ? -21.755 16.672  16.755  1.00 51.18  ? 401 A1EBZ A C12 1 
HETATM 5489 C C13 . A1EBZ C 2 .   ? -22.909 16.382  16.008  1.00 61.41  ? 401 A1EBZ A C13 1 
HETATM 5490 C C14 . A1EBZ C 2 .   ? -23.875 18.574  16.730  1.00 59.51  ? 401 A1EBZ A C14 1 
HETATM 5491 C C15 . A1EBZ C 2 .   ? -24.915 19.466  16.055  1.00 63.64  ? 401 A1EBZ A C15 1 
HETATM 5492 C C16 . A1EBZ C 2 .   ? -24.420 20.664  15.246  1.00 61.59  ? 401 A1EBZ A C16 1 
HETATM 5493 C C17 . A1EBZ C 2 .   ? -23.662 20.386  13.939  1.00 57.26  ? 401 A1EBZ A C17 1 
HETATM 5494 C C18 . A1EBZ C 2 .   ? -22.355 19.589  14.044  1.00 52.72  ? 401 A1EBZ A C18 1 
HETATM 5495 C C19 . A1EBZ C 2 .   ? -22.440 18.498  13.114  1.00 55.52  ? 401 A1EBZ A C19 1 
HETATM 5496 C C20 . A1EBZ C 2 .   ? -23.773 18.567  12.485  1.00 54.98  ? 401 A1EBZ A C20 1 
HETATM 5497 C C22 . A1EBZ C 2 .   ? -20.331 17.307  13.674  1.00 47.94  ? 401 A1EBZ A C22 1 
HETATM 5498 C C26 . A1EBZ C 2 .   ? -16.489 14.356  15.120  1.00 50.39  ? 401 A1EBZ A C26 1 
HETATM 5499 C C28 . A1EBZ C 2 .   ? -17.074 12.618  18.496  1.00 43.51  ? 401 A1EBZ A C28 1 
HETATM 5500 C C3  . A1EBZ C 2 .   ? -15.157 11.184  18.637  1.00 42.81  ? 401 A1EBZ A C3  1 
HETATM 5501 C C7  . A1EBZ C 2 .   ? -17.020 13.358  16.155  1.00 46.73  ? 401 A1EBZ A C7  1 
HETATM 5502 C C9  . A1EBZ C 2 .   ? -18.397 15.094  17.481  1.00 52.77  ? 401 A1EBZ A C9  1 
HETATM 5503 N N2  . A1EBZ C 2 .   ? -24.425 19.637  12.956  1.00 55.52  ? 401 A1EBZ A N2  1 
HETATM 5504 O O1  . A1EBZ C 2 .   ? -24.209 17.759  11.634  1.00 55.35  ? 401 A1EBZ A O1  1 
HETATM 5505 O O2  . A1EBZ C 2 .   ? -21.629 16.732  11.824  1.00 49.79  ? 401 A1EBZ A O2  1 
HETATM 5506 O O3  . A1EBZ C 2 .   ? -15.384 13.837  14.391  1.00 48.17  ? 401 A1EBZ A O3  1 
HETATM 5507 O O4  . A1EBZ C 2 .   ? -21.425 19.890  14.790  1.00 50.62  ? 401 A1EBZ A O4  1 
HETATM 5508 O O5  . A1EBZ C 2 .   ? -23.035 15.341  15.348  1.00 58.55  ? 401 A1EBZ A O5  1 
HETATM 5509 P PA  . NAP   D 3 .   ? -10.544 24.468  12.428  1.00 57.06  ? 402 NAP   A PA  1 
HETATM 5510 O O1A . NAP   D 3 .   ? -9.202  24.557  13.086  1.00 61.38  ? 402 NAP   A O1A 1 
HETATM 5511 O O2A . NAP   D 3 .   ? -10.728 24.864  10.992  1.00 62.73  ? 402 NAP   A O2A 1 
HETATM 5512 O O5B . NAP   D 3 .   ? -11.546 25.366  13.375  1.00 65.43  ? 402 NAP   A O5B 1 
HETATM 5513 C C5B . NAP   D 3 .   ? -11.205 26.722  13.660  1.00 66.00  ? 402 NAP   A C5B 1 
HETATM 5514 C C4B . NAP   D 3 .   ? -10.559 27.399  12.440  1.00 71.90  ? 402 NAP   A C4B 1 
HETATM 5515 O O4B . NAP   D 3 .   ? -11.527 27.861  11.480  1.00 67.89  ? 402 NAP   A O4B 1 
HETATM 5516 C C3B . NAP   D 3 .   ? -9.638  28.589  12.790  1.00 71.66  ? 402 NAP   A C3B 1 
HETATM 5517 O O3B . NAP   D 3 .   ? -8.280  28.215  12.821  1.00 65.44  ? 402 NAP   A O3B 1 
HETATM 5518 C C2B . NAP   D 3 .   ? -9.973  29.659  11.705  1.00 69.70  ? 402 NAP   A C2B 1 
HETATM 5519 O O2B . NAP   D 3 .   ? -8.885  29.757  10.835  1.00 64.09  ? 402 NAP   A O2B 1 
HETATM 5520 C C1B . NAP   D 3 .   ? -11.176 29.108  10.916  1.00 67.49  ? 402 NAP   A C1B 1 
HETATM 5521 N N9A . NAP   D 3 .   ? -12.341 29.993  10.801  1.00 65.41  ? 402 NAP   A N9A 1 
HETATM 5522 C C8A . NAP   D 3 .   ? -13.142 30.532  11.780  1.00 63.70  ? 402 NAP   A C8A 1 
HETATM 5523 N N7A . NAP   D 3 .   ? -14.110 31.271  11.320  1.00 58.54  ? 402 NAP   A N7A 1 
HETATM 5524 C C5A . NAP   D 3 .   ? -13.957 31.224  9.966   1.00 57.31  ? 402 NAP   A C5A 1 
HETATM 5525 C C6A . NAP   D 3 .   ? -14.687 31.804  8.913   1.00 62.33  ? 402 NAP   A C6A 1 
HETATM 5526 N N6A . NAP   D 3 .   ? -15.747 32.587  9.141   1.00 63.66  ? 402 NAP   A N6A 1 
HETATM 5527 N N1A . NAP   D 3 .   ? -14.272 31.573  7.655   1.00 59.89  ? 402 NAP   A N1A 1 
HETATM 5528 C C2A . NAP   D 3 .   ? -13.206 30.786  7.455   1.00 55.63  ? 402 NAP   A C2A 1 
HETATM 5529 N N3A . NAP   D 3 .   ? -12.446 30.186  8.363   1.00 63.14  ? 402 NAP   A N3A 1 
HETATM 5530 C C4A . NAP   D 3 .   ? -12.867 30.436  9.615   1.00 62.02  ? 402 NAP   A C4A 1 
HETATM 5531 O O3  . NAP   D 3 .   ? -11.116 22.926  12.508  1.00 59.50  ? 402 NAP   A O3  1 
HETATM 5532 P PN  . NAP   D 3 .   ? -10.473 21.578  11.781  1.00 58.89  ? 402 NAP   A PN  1 
HETATM 5533 O O1N . NAP   D 3 .   ? -9.629  20.797  12.741  1.00 53.74  ? 402 NAP   A O1N 1 
HETATM 5534 O O2N . NAP   D 3 .   ? -10.019 21.983  10.390  1.00 51.77  ? 402 NAP   A O2N 1 
HETATM 5535 O O5D . NAP   D 3 .   ? -11.854 20.694  11.610  1.00 55.46  ? 402 NAP   A O5D 1 
HETATM 5536 C C5D . NAP   D 3 .   ? -12.767 21.008  10.586  1.00 51.07  ? 402 NAP   A C5D 1 
HETATM 5537 C C4D . NAP   D 3 .   ? -14.154 21.347  11.124  1.00 50.92  ? 402 NAP   A C4D 1 
HETATM 5538 O O4D . NAP   D 3 .   ? -15.055 20.243  10.840  1.00 48.62  ? 402 NAP   A O4D 1 
HETATM 5539 C C3D . NAP   D 3 .   ? -14.222 21.598  12.624  1.00 49.90  ? 402 NAP   A C3D 1 
HETATM 5540 O O3D . NAP   D 3 .   ? -14.971 22.769  12.770  1.00 52.80  ? 402 NAP   A O3D 1 
HETATM 5541 C C2D . NAP   D 3 .   ? -15.037 20.424  13.187  1.00 47.98  ? 402 NAP   A C2D 1 
HETATM 5542 O O2D . NAP   D 3 .   ? -15.974 20.846  14.131  1.00 48.30  ? 402 NAP   A O2D 1 
HETATM 5543 C C1D . NAP   D 3 .   ? -15.760 19.848  11.952  1.00 47.15  ? 402 NAP   A C1D 1 
HETATM 5544 N N1N . NAP   D 3 .   ? -15.822 18.353  11.907  1.00 43.23  ? 402 NAP   A N1N 1 
HETATM 5545 C C2N . NAP   D 3 .   ? -16.784 17.690  11.236  1.00 40.09  ? 402 NAP   A C2N 1 
HETATM 5546 C C3N . NAP   D 3 .   ? -16.776 16.305  11.192  1.00 42.62  ? 402 NAP   A C3N 1 
HETATM 5547 C C7N . NAP   D 3 .   ? -17.812 15.462  10.486  1.00 40.94  ? 402 NAP   A C7N 1 
HETATM 5548 O O7N . NAP   D 3 .   ? -17.776 14.239  10.599  1.00 38.61  ? 402 NAP   A O7N 1 
HETATM 5549 N N7N . NAP   D 3 .   ? -18.720 16.132  9.764   1.00 42.95  ? 402 NAP   A N7N 1 
HETATM 5550 C C4N . NAP   D 3 .   ? -15.747 15.639  11.853  1.00 46.71  ? 402 NAP   A C4N 1 
HETATM 5551 C C5N . NAP   D 3 .   ? -14.776 16.356  12.536  1.00 46.54  ? 402 NAP   A C5N 1 
HETATM 5552 C C6N . NAP   D 3 .   ? -14.829 17.725  12.535  1.00 41.80  ? 402 NAP   A C6N 1 
HETATM 5553 P P2B . NAP   D 3 .   ? -8.031  31.268  10.853  1.00 66.61  ? 402 NAP   A P2B 1 
HETATM 5554 O O1X . NAP   D 3 .   ? -9.179  32.272  10.752  1.00 68.78  ? 402 NAP   A O1X 1 
HETATM 5555 O O2X . NAP   D 3 .   ? -7.368  31.135  12.217  1.00 68.85  ? 402 NAP   A O2X 1 
HETATM 5556 O O3X . NAP   D 3 .   ? -7.081  31.258  9.654   1.00 50.84  ? 402 NAP   A O3X 1 
HETATM 5557 C C8  . A1EBZ E 2 .   ? -33.014 21.440  -21.903 1.00 40.51  ? 401 A1EBZ B C8  1 
HETATM 5558 C C5  . A1EBZ E 2 .   ? -35.358 17.560  -23.774 1.00 43.17  ? 401 A1EBZ B C5  1 
HETATM 5559 C C6  . A1EBZ E 2 .   ? -34.280 19.881  -23.283 1.00 34.47  ? 401 A1EBZ B C6  1 
HETATM 5560 N N1  . A1EBZ E 2 .   ? -31.086 26.703  -18.234 1.00 46.58  ? 401 A1EBZ B N1  1 
HETATM 5561 C C2  . A1EBZ E 2 .   ? -33.602 17.909  -26.541 1.00 41.82  ? 401 A1EBZ B C2  1 
HETATM 5562 C C4  . A1EBZ E 2 .   ? -34.222 18.534  -24.057 1.00 42.95  ? 401 A1EBZ B C4  1 
HETATM 5563 C C21 . A1EBZ E 2 .   ? -32.357 23.163  -16.110 1.00 40.78  ? 401 A1EBZ B C21 1 
HETATM 5564 C C23 . A1EBZ E 2 .   ? -33.001 21.467  -17.675 1.00 43.89  ? 401 A1EBZ B C23 1 
HETATM 5565 C C24 . A1EBZ E 2 .   ? -33.747 20.957  -18.773 1.00 41.60  ? 401 A1EBZ B C24 1 
HETATM 5566 C C25 . A1EBZ E 2 .   ? -33.613 19.816  -19.422 1.00 38.84  ? 401 A1EBZ B C25 1 
HETATM 5567 C C27 . A1EBZ E 2 .   ? -32.539 21.620  -23.348 1.00 41.46  ? 401 A1EBZ B C27 1 
HETATM 5568 C C29 . A1EBZ E 2 .   ? -33.073 20.176  -25.411 1.00 35.12  ? 401 A1EBZ B C29 1 
HETATM 5569 C C1  . A1EBZ E 2 .   ? -33.294 18.483  -27.904 1.00 39.27  ? 401 A1EBZ B C1  1 
HETATM 5570 C C10 . A1EBZ E 2 .   ? -33.871 23.595  -20.729 1.00 43.22  ? 401 A1EBZ B C10 1 
HETATM 5571 C C11 . A1EBZ E 2 .   ? -32.701 24.059  -20.019 1.00 41.99  ? 401 A1EBZ B C11 1 
HETATM 5572 C C12 . A1EBZ E 2 .   ? -32.486 25.201  -19.364 1.00 43.15  ? 401 A1EBZ B C12 1 
HETATM 5573 C C13 . A1EBZ E 2 .   ? -31.276 25.471  -18.733 1.00 46.28  ? 401 A1EBZ B C13 1 
HETATM 5574 C C14 . A1EBZ E 2 .   ? -32.129 27.667  -17.928 1.00 48.46  ? 401 A1EBZ B C14 1 
HETATM 5575 C C15 . A1EBZ E 2 .   ? -31.714 28.051  -16.505 1.00 42.60  ? 401 A1EBZ B C15 1 
HETATM 5576 C C16 . A1EBZ E 2 .   ? -32.776 27.988  -15.424 1.00 35.02  ? 401 A1EBZ B C16 1 
HETATM 5577 C C17 . A1EBZ E 2 .   ? -32.992 26.615  -14.782 1.00 37.52  ? 401 A1EBZ B C17 1 
HETATM 5578 C C18 . A1EBZ E 2 .   ? -33.415 25.453  -15.690 1.00 39.79  ? 401 A1EBZ B C18 1 
HETATM 5579 C C19 . A1EBZ E 2 .   ? -32.431 24.414  -15.535 1.00 38.74  ? 401 A1EBZ B C19 1 
HETATM 5580 C C20 . A1EBZ E 2 .   ? -31.452 24.878  -14.565 1.00 40.02  ? 401 A1EBZ B C20 1 
HETATM 5581 C C22 . A1EBZ E 2 .   ? -33.151 22.712  -17.141 1.00 40.82  ? 401 A1EBZ B C22 1 
HETATM 5582 C C26 . A1EBZ E 2 .   ? -34.380 19.590  -20.686 1.00 40.83  ? 401 A1EBZ B C26 1 
HETATM 5583 C C28 . A1EBZ E 2 .   ? -33.622 20.953  -24.205 1.00 37.42  ? 401 A1EBZ B C28 1 
HETATM 5584 C C3  . A1EBZ E 2 .   ? -34.036 18.976  -25.534 1.00 42.61  ? 401 A1EBZ B C3  1 
HETATM 5585 C C7  . A1EBZ E 2 .   ? -33.552 19.985  -21.920 1.00 39.27  ? 401 A1EBZ B C7  1 
HETATM 5586 C C9  . A1EBZ E 2 .   ? -34.010 22.490  -21.508 1.00 44.50  ? 401 A1EBZ B C9  1 
HETATM 5587 N N2  . A1EBZ E 2 .   ? -31.804 26.094  -14.127 1.00 43.19  ? 401 A1EBZ B N2  1 
HETATM 5588 O O1  . A1EBZ E 2 .   ? -30.481 24.187  -14.186 1.00 41.26  ? 401 A1EBZ B O1  1 
HETATM 5589 O O2  . A1EBZ E 2 .   ? -31.470 22.300  -15.638 1.00 41.94  ? 401 A1EBZ B O2  1 
HETATM 5590 O O3  . A1EBZ E 2 .   ? -34.952 18.289  -20.715 1.00 43.36  ? 401 A1EBZ B O3  1 
HETATM 5591 O O4  . A1EBZ E 2 .   ? -34.434 25.460  -16.379 1.00 37.76  ? 401 A1EBZ B O4  1 
HETATM 5592 O O5  . A1EBZ E 2 .   ? -30.479 24.551  -18.482 1.00 52.13  ? 401 A1EBZ B O5  1 
HETATM 5593 P PA  . NAP   F 3 .   ? -44.815 18.733  -14.936 1.00 48.90  ? 402 NAP   B PA  1 
HETATM 5594 O O1A . NAP   F 3 .   ? -46.078 18.320  -15.618 1.00 46.46  ? 402 NAP   B O1A 1 
HETATM 5595 O O2A . NAP   F 3 .   ? -44.385 18.181  -13.599 1.00 51.02  ? 402 NAP   B O2A 1 
HETATM 5596 O O5B . NAP   F 3 .   ? -44.804 20.364  -14.835 1.00 43.81  ? 402 NAP   B O5B 1 
HETATM 5597 C C5B . NAP   F 3 .   ? -45.963 21.104  -14.524 1.00 45.70  ? 402 NAP   B C5B 1 
HETATM 5598 C C4B . NAP   F 3 .   ? -46.769 20.470  -13.392 1.00 52.41  ? 402 NAP   B C4B 1 
HETATM 5599 O O4B . NAP   F 3 .   ? -46.162 20.664  -12.105 1.00 55.07  ? 402 NAP   B O4B 1 
HETATM 5600 C C3B . NAP   F 3 .   ? -48.173 21.094  -13.308 1.00 53.94  ? 402 NAP   B C3B 1 
HETATM 5601 O O3B . NAP   F 3 .   ? -49.091 20.437  -14.138 1.00 60.24  ? 402 NAP   B O3B 1 
HETATM 5602 C C2B . NAP   F 3 .   ? -48.510 20.989  -11.805 1.00 53.07  ? 402 NAP   B C2B 1 
HETATM 5603 O O2B . NAP   F 3 .   ? -49.169 19.773  -11.637 1.00 57.81  ? 402 NAP   B O2B 1 
HETATM 5604 C C1B . NAP   F 3 .   ? -47.139 20.893  -11.110 1.00 52.15  ? 402 NAP   B C1B 1 
HETATM 5605 N N9A . NAP   F 3 .   ? -46.839 22.003  -10.197 1.00 49.49  ? 402 NAP   B N9A 1 
HETATM 5606 C C8A . NAP   F 3 .   ? -46.906 23.365  -10.367 1.00 44.21  ? 402 NAP   B C8A 1 
HETATM 5607 N N7A . NAP   F 3 .   ? -46.573 24.051  -9.307  1.00 40.91  ? 402 NAP   B N7A 1 
HETATM 5608 C C5A . NAP   F 3 .   ? -46.272 23.098  -8.364  1.00 45.50  ? 402 NAP   B C5A 1 
HETATM 5609 C C6A . NAP   F 3 .   ? -45.835 23.167  -7.018  1.00 42.16  ? 402 NAP   B C6A 1 
HETATM 5610 N N6A . NAP   F 3 .   ? -45.621 24.310  -6.363  1.00 43.46  ? 402 NAP   B N6A 1 
HETATM 5611 N N1A . NAP   F 3 .   ? -45.616 22.020  -6.376  1.00 44.45  ? 402 NAP   B N1A 1 
HETATM 5612 C C2A . NAP   F 3 .   ? -45.809 20.855  -7.012  1.00 47.99  ? 402 NAP   B C2A 1 
HETATM 5613 N N3A . NAP   F 3 .   ? -46.213 20.657  -8.262  1.00 51.85  ? 402 NAP   B N3A 1 
HETATM 5614 C C4A . NAP   F 3 .   ? -46.432 21.820  -8.900  1.00 50.54  ? 402 NAP   B C4A 1 
HETATM 5615 O O3  . NAP   F 3 .   ? -43.538 18.525  -15.944 1.00 45.11  ? 402 NAP   B O3  1 
HETATM 5616 P PN  . NAP   F 3 .   ? -42.727 17.144  -16.283 1.00 49.38  ? 402 NAP   B PN  1 
HETATM 5617 O O1N . NAP   F 3 .   ? -42.695 16.939  -17.763 1.00 47.98  ? 402 NAP   B O1N 1 
HETATM 5618 O O2N . NAP   F 3 .   ? -43.244 16.114  -15.313 1.00 52.55  ? 402 NAP   B O2N 1 
HETATM 5619 O O5D . NAP   F 3 .   ? -41.182 17.531  -15.815 1.00 48.58  ? 402 NAP   B O5D 1 
HETATM 5620 C C5D . NAP   F 3 .   ? -40.824 17.672  -14.462 1.00 46.01  ? 402 NAP   B C5D 1 
HETATM 5621 C C4D . NAP   F 3 .   ? -40.014 18.932  -14.125 1.00 45.66  ? 402 NAP   B C4D 1 
HETATM 5622 O O4D . NAP   F 3 .   ? -38.602 18.727  -14.431 1.00 50.16  ? 402 NAP   B O4D 1 
HETATM 5623 C C3D . NAP   F 3 .   ? -40.377 20.213  -14.861 1.00 44.58  ? 402 NAP   B C3D 1 
HETATM 5624 O O3D . NAP   F 3 .   ? -40.130 21.258  -13.940 1.00 42.62  ? 402 NAP   B O3D 1 
HETATM 5625 C C2D . NAP   F 3 .   ? -39.366 20.211  -16.035 1.00 42.86  ? 402 NAP   B C2D 1 
HETATM 5626 O O2D . NAP   F 3 .   ? -39.120 21.450  -16.634 1.00 38.42  ? 402 NAP   B O2D 1 
HETATM 5627 C C1D . NAP   F 3 .   ? -38.111 19.684  -15.304 1.00 46.45  ? 402 NAP   B C1D 1 
HETATM 5628 N N1N . NAP   F 3 .   ? -37.041 19.029  -16.145 1.00 40.64  ? 402 NAP   B N1N 1 
HETATM 5629 C C2N . NAP   F 3 .   ? -35.753 19.036  -15.761 1.00 39.67  ? 402 NAP   B C2N 1 
HETATM 5630 C C3N . NAP   F 3 .   ? -34.786 18.398  -16.531 1.00 44.38  ? 402 NAP   B C3N 1 
HETATM 5631 C C7N . NAP   F 3 .   ? -33.336 18.372  -16.116 1.00 39.77  ? 402 NAP   B C7N 1 
HETATM 5632 O O7N . NAP   F 3 .   ? -32.490 17.947  -16.879 1.00 39.40  ? 402 NAP   B O7N 1 
HETATM 5633 N N7N . NAP   F 3 .   ? -33.089 18.807  -14.882 1.00 34.78  ? 402 NAP   B N7N 1 
HETATM 5634 C C4N . NAP   F 3 .   ? -35.164 17.732  -17.700 1.00 38.35  ? 402 NAP   B C4N 1 
HETATM 5635 C C5N . NAP   F 3 .   ? -36.491 17.744  -18.080 1.00 35.27  ? 402 NAP   B C5N 1 
HETATM 5636 C C6N . NAP   F 3 .   ? -37.405 18.394  -17.274 1.00 40.88  ? 402 NAP   B C6N 1 
HETATM 5637 P P2B . NAP   F 3 .   ? -50.701 19.776  -10.832 1.00 56.74  ? 402 NAP   B P2B 1 
HETATM 5638 O O1X . NAP   F 3 .   ? -50.727 21.067  -10.012 1.00 47.67  ? 402 NAP   B O1X 1 
HETATM 5639 O O2X . NAP   F 3 .   ? -51.605 19.728  -12.060 1.00 51.70  ? 402 NAP   B O2X 1 
HETATM 5640 O O3X . NAP   F 3 .   ? -50.598 18.480  -10.041 1.00 51.26  ? 402 NAP   B O3X 1 
HETATM 5641 O O   . HOH   G 4 .   ? -7.598  23.890  -12.219 1.00 34.42  ? 501 HOH   A O   1 
HETATM 5642 O O   . HOH   G 4 .   ? -18.053 25.680  24.242  1.00 43.25  ? 502 HOH   A O   1 
HETATM 5643 O O   . HOH   G 4 .   ? 2.822   -2.723  19.814  1.00 45.48  ? 503 HOH   A O   1 
HETATM 5644 O O   . HOH   G 4 .   ? -23.064 5.818   7.051   1.00 36.47  ? 504 HOH   A O   1 
HETATM 5645 O O   . HOH   G 4 .   ? -21.622 26.930  -12.623 1.00 37.97  ? 505 HOH   A O   1 
HETATM 5646 O O   . HOH   G 4 .   ? 14.238  10.640  17.793  1.00 45.66  ? 506 HOH   A O   1 
HETATM 5647 O O   . HOH   G 4 .   ? -9.643  10.660  17.644  1.00 29.59  ? 507 HOH   A O   1 
HETATM 5648 O O   . HOH   G 4 .   ? -14.230 -0.483  6.922   1.00 46.65  ? 508 HOH   A O   1 
HETATM 5649 O O   . HOH   G 4 .   ? -19.408 -4.168  33.329  1.00 43.20  ? 509 HOH   A O   1 
HETATM 5650 O O   . HOH   G 4 .   ? 4.055   13.452  25.496  1.00 37.51  ? 510 HOH   A O   1 
HETATM 5651 O O   . HOH   G 4 .   ? -4.204  12.829  -3.006  1.00 26.17  ? 511 HOH   A O   1 
HETATM 5652 O O   . HOH   G 4 .   ? -21.532 20.626  17.238  1.00 45.02  ? 512 HOH   A O   1 
HETATM 5653 O O   . HOH   G 4 .   ? -20.468 16.883  27.051  1.00 43.27  ? 513 HOH   A O   1 
HETATM 5654 O O   . HOH   G 4 .   ? -3.324  2.761   17.336  1.00 38.05  ? 514 HOH   A O   1 
HETATM 5655 O O   . HOH   G 4 .   ? -5.641  12.849  -9.276  1.00 33.41  ? 515 HOH   A O   1 
HETATM 5656 O O   . HOH   G 4 .   ? -4.614  5.936   15.716  1.00 32.75  ? 516 HOH   A O   1 
HETATM 5657 O O   . HOH   G 4 .   ? -12.978 26.573  37.569  1.00 43.15  ? 517 HOH   A O   1 
HETATM 5658 O O   . HOH   G 4 .   ? 6.830   2.463   16.438  1.00 35.90  ? 518 HOH   A O   1 
HETATM 5659 O O   . HOH   G 4 .   ? 1.053   4.288   11.918  1.00 39.15  ? 519 HOH   A O   1 
HETATM 5660 O O   . HOH   G 4 .   ? 3.309   15.401  20.687  1.00 46.91  ? 520 HOH   A O   1 
HETATM 5661 O O   . HOH   G 4 .   ? -9.695  14.413  18.300  1.00 36.08  ? 521 HOH   A O   1 
HETATM 5662 O O   . HOH   G 4 .   ? -11.940 32.326  28.295  1.00 42.24  ? 522 HOH   A O   1 
HETATM 5663 O O   . HOH   G 4 .   ? -21.330 15.235  29.096  1.00 47.46  ? 523 HOH   A O   1 
HETATM 5664 O O   . HOH   G 4 .   ? -11.919 22.678  6.304   1.00 38.19  ? 524 HOH   A O   1 
HETATM 5665 O O   . HOH   G 4 .   ? -18.329 5.686   2.891   1.00 39.44  ? 525 HOH   A O   1 
HETATM 5666 O O   . HOH   G 4 .   ? -27.720 35.174  17.273  1.00 52.34  ? 526 HOH   A O   1 
HETATM 5667 O O   . HOH   G 4 .   ? 2.113   9.852   26.221  1.00 30.43  ? 527 HOH   A O   1 
HETATM 5668 O O   . HOH   G 4 .   ? 12.537  7.376   19.151  1.00 37.11  ? 528 HOH   A O   1 
HETATM 5669 O O   . HOH   G 4 .   ? -20.536 36.641  5.463   1.00 59.91  ? 529 HOH   A O   1 
HETATM 5670 O O   . HOH   G 4 .   ? -12.951 16.258  20.993  1.00 32.25  ? 530 HOH   A O   1 
HETATM 5671 O O   . HOH   G 4 .   ? -30.241 27.860  -12.328 1.00 38.86  ? 531 HOH   A O   1 
HETATM 5672 O O   . HOH   G 4 .   ? -18.995 10.550  5.968   1.00 31.87  ? 532 HOH   A O   1 
HETATM 5673 O O   . HOH   G 4 .   ? -19.653 12.026  -6.385  1.00 34.72  ? 533 HOH   A O   1 
HETATM 5674 O O   . HOH   G 4 .   ? -31.154 25.906  -1.116  1.00 44.14  ? 534 HOH   A O   1 
HETATM 5675 O O   . HOH   G 4 .   ? -11.095 11.673  29.030  1.00 33.09  ? 535 HOH   A O   1 
HETATM 5676 O O   . HOH   G 4 .   ? -13.238 21.029  -15.093 1.00 39.68  ? 536 HOH   A O   1 
HETATM 5677 O O   . HOH   G 4 .   ? 3.976   16.436  9.989   1.00 43.56  ? 537 HOH   A O   1 
HETATM 5678 O O   . HOH   G 4 .   ? -15.051 17.372  -10.682 1.00 25.68  ? 538 HOH   A O   1 
HETATM 5679 O O   . HOH   G 4 .   ? -20.976 5.416   3.201   1.00 41.48  ? 539 HOH   A O   1 
HETATM 5680 O O   . HOH   G 4 .   ? -2.518  -0.274  24.531  1.00 30.86  ? 540 HOH   A O   1 
HETATM 5681 O O   . HOH   G 4 .   ? -10.626 4.676   1.596   1.00 27.50  ? 541 HOH   A O   1 
HETATM 5682 O O   . HOH   G 4 .   ? -15.547 19.512  -12.406 1.00 30.37  ? 542 HOH   A O   1 
HETATM 5683 O O   . HOH   G 4 .   ? -9.384  27.838  -11.603 1.00 41.38  ? 543 HOH   A O   1 
HETATM 5684 O O   . HOH   G 4 .   ? -0.136  12.833  29.581  1.00 34.93  ? 544 HOH   A O   1 
HETATM 5685 O O   . HOH   G 4 .   ? 5.103   15.569  8.190   1.00 43.36  ? 545 HOH   A O   1 
HETATM 5686 O O   . HOH   G 4 .   ? -24.628 26.639  3.213   1.00 38.84  ? 546 HOH   A O   1 
HETATM 5687 O O   . HOH   G 4 .   ? -5.372  12.443  34.253  1.00 37.64  ? 547 HOH   A O   1 
HETATM 5688 O O   . HOH   G 4 .   ? -16.799 7.975   35.635  1.00 37.06  ? 548 HOH   A O   1 
HETATM 5689 O O   . HOH   G 4 .   ? -13.386 5.526   20.043  1.00 36.27  ? 549 HOH   A O   1 
HETATM 5690 O O   . HOH   G 4 .   ? -11.453 8.837   -4.862  1.00 46.70  ? 550 HOH   A O   1 
HETATM 5691 O O   . HOH   G 4 .   ? -12.544 5.709   17.528  1.00 34.03  ? 551 HOH   A O   1 
HETATM 5692 O O   . HOH   G 4 .   ? -14.396 -2.547  13.141  1.00 45.13  ? 552 HOH   A O   1 
HETATM 5693 O O   . HOH   G 4 .   ? -9.377  12.943  -4.224  1.00 39.27  ? 553 HOH   A O   1 
HETATM 5694 O O   . HOH   G 4 .   ? -13.102 -3.520  10.008  1.00 50.91  ? 554 HOH   A O   1 
HETATM 5695 O O   . HOH   G 4 .   ? -1.874  15.027  14.690  1.00 33.62  ? 555 HOH   A O   1 
HETATM 5696 O O   . HOH   G 4 .   ? 4.479   8.102   21.101  1.00 39.09  ? 556 HOH   A O   1 
HETATM 5697 O O   . HOH   G 4 .   ? 0.734   -1.301  22.501  1.00 34.47  ? 557 HOH   A O   1 
HETATM 5698 O O   . HOH   G 4 .   ? -17.531 14.286  44.936  1.00 45.34  ? 558 HOH   A O   1 
HETATM 5699 O O   . HOH   G 4 .   ? -29.312 26.443  30.190  1.00 45.86  ? 559 HOH   A O   1 
HETATM 5700 O O   . HOH   G 4 .   ? -15.932 2.413   5.011   1.00 35.10  ? 560 HOH   A O   1 
HETATM 5701 O O   . HOH   G 4 .   ? -10.986 0.582   3.641   1.00 37.52  ? 561 HOH   A O   1 
HETATM 5702 O O   . HOH   G 4 .   ? -2.041  32.284  -7.355  1.00 50.45  ? 562 HOH   A O   1 
HETATM 5703 O O   . HOH   G 4 .   ? 11.152  7.857   16.076  1.00 47.18  ? 563 HOH   A O   1 
HETATM 5704 O O   . HOH   G 4 .   ? -11.243 33.075  -16.877 1.00 47.75  ? 564 HOH   A O   1 
HETATM 5705 O O   . HOH   G 4 .   ? -13.376 3.007   16.319  1.00 37.87  ? 565 HOH   A O   1 
HETATM 5706 O O   . HOH   G 4 .   ? -23.607 7.543   14.919  1.00 39.91  ? 566 HOH   A O   1 
HETATM 5707 O O   . HOH   G 4 .   ? -20.732 26.614  23.802  1.00 44.29  ? 567 HOH   A O   1 
HETATM 5708 O O   . HOH   G 4 .   ? -24.226 30.587  -12.097 1.00 42.64  ? 568 HOH   A O   1 
HETATM 5709 O O   . HOH   G 4 .   ? -8.167  -8.128  26.669  1.00 49.05  ? 569 HOH   A O   1 
HETATM 5710 O O   . HOH   G 4 .   ? -16.525 22.910  -16.508 1.00 31.91  ? 570 HOH   A O   1 
HETATM 5711 O O   . HOH   G 4 .   ? -29.146 21.335  27.674  1.00 54.82  ? 571 HOH   A O   1 
HETATM 5712 O O   . HOH   G 4 .   ? 2.994   16.057  23.915  1.00 43.28  ? 572 HOH   A O   1 
HETATM 5713 O O   . HOH   G 4 .   ? -6.245  14.654  39.866  1.00 51.39  ? 573 HOH   A O   1 
HETATM 5714 O O   . HOH   G 4 .   ? -29.564 30.193  -12.003 1.00 40.34  ? 574 HOH   A O   1 
HETATM 5715 O O   . HOH   G 4 .   ? -23.884 9.960   -6.005  1.00 37.30  ? 575 HOH   A O   1 
HETATM 5716 O O   . HOH   H 4 .   ? -44.572 20.809  -47.212 1.00 45.56  ? 501 HOH   B O   1 
HETATM 5717 O O   . HOH   H 4 .   ? -31.747 29.956  -20.853 1.00 35.76  ? 502 HOH   B O   1 
HETATM 5718 O O   . HOH   H 4 .   ? -32.574 14.174  8.786   1.00 41.79  ? 503 HOH   B O   1 
HETATM 5719 O O   . HOH   H 4 .   ? -27.947 4.846   -1.178  1.00 47.11  ? 504 HOH   B O   1 
HETATM 5720 O O   . HOH   H 4 .   ? -42.829 34.234  -17.694 1.00 39.33  ? 505 HOH   B O   1 
HETATM 5721 O O   . HOH   H 4 .   ? -35.611 27.168  -17.665 1.00 39.56  ? 506 HOH   B O   1 
HETATM 5722 O O   . HOH   H 4 .   ? -27.851 14.273  -15.202 1.00 28.61  ? 507 HOH   B O   1 
HETATM 5723 O O   . HOH   H 4 .   ? -46.317 2.392   2.433   1.00 45.89  ? 508 HOH   B O   1 
HETATM 5724 O O   . HOH   H 4 .   ? -32.365 23.417  -34.420 1.00 46.81  ? 509 HOH   B O   1 
HETATM 5725 O O   . HOH   H 4 .   ? -21.948 15.206  -17.504 1.00 26.19  ? 510 HOH   B O   1 
HETATM 5726 O O   . HOH   H 4 .   ? -31.625 15.668  -30.369 1.00 39.83  ? 511 HOH   B O   1 
HETATM 5727 O O   . HOH   H 4 .   ? -45.426 11.074  -25.720 1.00 52.82  ? 512 HOH   B O   1 
HETATM 5728 O O   . HOH   H 4 .   ? -32.212 32.871  -30.162 1.00 32.46  ? 513 HOH   B O   1 
HETATM 5729 O O   . HOH   H 4 .   ? -39.484 21.591  -24.869 1.00 37.20  ? 514 HOH   B O   1 
HETATM 5730 O O   . HOH   H 4 .   ? -25.465 6.204   -7.285  1.00 41.70  ? 515 HOH   B O   1 
HETATM 5731 O O   . HOH   H 4 .   ? -39.371 18.258  -22.764 1.00 38.64  ? 516 HOH   B O   1 
HETATM 5732 O O   . HOH   H 4 .   ? -39.556 16.527  -24.984 1.00 34.65  ? 517 HOH   B O   1 
HETATM 5733 O O   . HOH   H 4 .   ? -35.282 25.942  -31.798 1.00 25.07  ? 518 HOH   B O   1 
HETATM 5734 O O   . HOH   H 4 .   ? -37.004 35.701  -36.013 1.00 31.30  ? 519 HOH   B O   1 
HETATM 5735 O O   . HOH   H 4 .   ? -48.974 17.818  -14.201 1.00 44.08  ? 520 HOH   B O   1 
HETATM 5736 O O   . HOH   H 4 .   ? -46.200 18.085  -20.160 1.00 45.73  ? 521 HOH   B O   1 
HETATM 5737 O O   . HOH   H 4 .   ? -54.019 24.582  -12.985 1.00 50.10  ? 522 HOH   B O   1 
HETATM 5738 O O   . HOH   H 4 .   ? -51.506 22.846  -37.234 1.00 39.25  ? 523 HOH   B O   1 
HETATM 5739 O O   . HOH   H 4 .   ? -54.759 24.263  -36.791 1.00 55.32  ? 524 HOH   B O   1 
HETATM 5740 O O   . HOH   H 4 .   ? -28.523 24.749  -12.437 1.00 34.50  ? 525 HOH   B O   1 
HETATM 5741 O O   . HOH   H 4 .   ? -39.434 42.324  -23.324 1.00 38.27  ? 526 HOH   B O   1 
HETATM 5742 O O   . HOH   H 4 .   ? -51.628 28.383  -37.682 1.00 44.42  ? 527 HOH   B O   1 
HETATM 5743 O O   . HOH   H 4 .   ? -40.952 33.153  -19.736 1.00 35.72  ? 528 HOH   B O   1 
HETATM 5744 O O   . HOH   H 4 .   ? -39.897 22.314  -34.645 1.00 28.21  ? 529 HOH   B O   1 
HETATM 5745 O O   . HOH   H 4 .   ? -35.170 32.781  -34.259 1.00 37.29  ? 530 HOH   B O   1 
HETATM 5746 O O   . HOH   H 4 .   ? -29.609 11.877  -28.646 1.00 37.82  ? 531 HOH   B O   1 
HETATM 5747 O O   . HOH   H 4 .   ? -28.570 3.024   -16.611 1.00 42.06  ? 532 HOH   B O   1 
HETATM 5748 O O   . HOH   H 4 .   ? -35.753 26.365  -4.710  1.00 37.51  ? 533 HOH   B O   1 
HETATM 5749 O O   . HOH   H 4 .   ? -42.514 43.066  -29.412 1.00 39.18  ? 534 HOH   B O   1 
HETATM 5750 O O   . HOH   H 4 .   ? -34.293 38.955  -32.933 1.00 26.49  ? 535 HOH   B O   1 
HETATM 5751 O O   . HOH   H 4 .   ? -53.006 19.095  -37.202 1.00 40.88  ? 536 HOH   B O   1 
HETATM 5752 O O   . HOH   H 4 .   ? -35.557 30.214  -27.708 1.00 29.73  ? 537 HOH   B O   1 
HETATM 5753 O O   . HOH   H 4 .   ? -26.303 9.120   0.547   1.00 37.68  ? 538 HOH   B O   1 
HETATM 5754 O O   . HOH   H 4 .   ? -54.646 28.182  -22.192 1.00 39.47  ? 539 HOH   B O   1 
HETATM 5755 O O   . HOH   H 4 .   ? -26.575 17.579  9.854   1.00 36.70  ? 540 HOH   B O   1 
HETATM 5756 O O   . HOH   H 4 .   ? -52.568 29.839  -28.503 1.00 41.81  ? 541 HOH   B O   1 
HETATM 5757 O O   . HOH   H 4 .   ? -35.215 25.383  -11.811 1.00 37.27  ? 542 HOH   B O   1 
HETATM 5758 O O   . HOH   H 4 .   ? -31.970 13.654  -28.608 1.00 41.85  ? 543 HOH   B O   1 
HETATM 5759 O O   . HOH   H 4 .   ? -55.246 29.219  -28.600 1.00 46.19  ? 544 HOH   B O   1 
HETATM 5760 O O   . HOH   H 4 .   ? -34.341 31.162  -30.418 1.00 32.46  ? 545 HOH   B O   1 
HETATM 5761 O O   . HOH   H 4 .   ? -25.482 15.545  -29.532 1.00 37.00  ? 546 HOH   B O   1 
HETATM 5762 O O   . HOH   H 4 .   ? -47.483 37.466  -39.948 1.00 33.27  ? 547 HOH   B O   1 
HETATM 5763 O O   . HOH   H 4 .   ? -42.623 31.874  -21.293 1.00 36.94  ? 548 HOH   B O   1 
HETATM 5764 O O   . HOH   H 4 .   ? -28.330 28.087  -20.306 1.00 41.34  ? 549 HOH   B O   1 
HETATM 5765 O O   . HOH   H 4 .   ? -42.544 38.451  -10.697 1.00 51.58  ? 550 HOH   B O   1 
HETATM 5766 O O   . HOH   H 4 .   ? -39.268 29.236  -40.478 1.00 37.78  ? 551 HOH   B O   1 
HETATM 5767 O O   . HOH   H 4 .   ? -42.140 6.535   5.820   1.00 62.36  ? 552 HOH   B O   1 
HETATM 5768 O O   . HOH   H 4 .   ? -50.303 36.281  -32.712 1.00 30.00  ? 553 HOH   B O   1 
HETATM 5769 O O   . HOH   H 4 .   ? -24.824 21.011  -22.649 1.00 38.79  ? 554 HOH   B O   1 
HETATM 5770 O O   . HOH   H 4 .   ? -40.789 35.847  -21.078 1.00 33.08  ? 555 HOH   B O   1 
HETATM 5771 O O   . HOH   H 4 .   ? -21.537 14.257  -13.079 1.00 40.83  ? 556 HOH   B O   1 
HETATM 5772 O O   . HOH   H 4 .   ? -33.776 41.172  -26.476 1.00 36.64  ? 557 HOH   B O   1 
HETATM 5773 O O   . HOH   H 4 .   ? -24.201 7.660   -19.529 1.00 40.58  ? 558 HOH   B O   1 
HETATM 5774 O O   . HOH   H 4 .   ? -46.033 3.528   -35.773 1.00 56.00  ? 559 HOH   B O   1 
HETATM 5775 O O   . HOH   H 4 .   ? -22.936 26.919  -31.896 1.00 43.45  ? 560 HOH   B O   1 
HETATM 5776 O O   . HOH   H 4 .   ? -25.113 8.628   -3.773  1.00 45.97  ? 561 HOH   B O   1 
HETATM 5777 O O   . HOH   H 4 .   ? -48.518 15.924  -37.433 1.00 49.90  ? 562 HOH   B O   1 
HETATM 5778 O O   . HOH   H 4 .   ? -29.176 32.896  -28.914 1.00 40.42  ? 563 HOH   B O   1 
HETATM 5779 O O   . HOH   H 4 .   ? -28.138 25.344  -39.545 1.00 47.37  ? 564 HOH   B O   1 
HETATM 5780 O O   . HOH   H 4 .   ? -29.346 26.626  0.874   1.00 46.00  ? 565 HOH   B O   1 
HETATM 5781 O O   . HOH   H 4 .   ? -47.065 31.108  -8.684  1.00 40.29  ? 566 HOH   B O   1 
HETATM 5782 O O   . HOH   H 4 .   ? -47.193 4.977   -34.312 1.00 54.39  ? 567 HOH   B O   1 
HETATM 5783 O O   . HOH   H 4 .   ? -46.990 32.147  -51.275 1.00 31.52  ? 568 HOH   B O   1 
HETATM 5784 O O   . HOH   H 4 .   ? -33.561 18.122  12.179  1.00 47.78  ? 569 HOH   B O   1 
HETATM 5785 O O   . HOH   H 4 .   ? -33.427 34.473  3.573   1.00 51.75  ? 570 HOH   B O   1 
HETATM 5786 O O   . HOH   H 4 .   ? -57.010 9.755   -15.634 1.00 49.46  ? 571 HOH   B O   1 
HETATM 5787 O O   . HOH   H 4 .   ? -33.564 28.221  -27.403 1.00 27.66  ? 572 HOH   B O   1 
HETATM 5788 O O   . HOH   H 4 .   ? -29.064 21.511  12.681  1.00 49.17  ? 573 HOH   B O   1 
# 
